Graduate Study in - Chemistry - Johns Hopkins University

Chemistry
Graduate Study in
www.jhu.edu/~chem

Contents
2 Welcome
3 Baltimore
4 Johns Hopkins University
5 Department of Chemistry
7 Faculty
7 Kit H. Bowen
8 Paul J. Dagdigian
9 David E. Draper
10 D. Howard Fairbrother
11 David P. Goldberg
12 Marc M. Greenberg
13 Tamara L Hendrickson
14 Kenneth D. Karlin
15 Thomas Lectka
16 Gerald J. Meyer
17 Douglas Poland
18 Gary H. Posner
19 Harris J. Silverstone
20 Joel R. Tolman
21 John P. Toscano
22 Craig A. Townsend
23 David R. Yarkony
24 Instrumentation
26 Useful Information
28 Baltimore Map & Directions to Campus
Graduate Study in
Chemistry at The Johns Hopkins University
1

Welcome
Rendition of new chemistry
building currently under
construction
Greetings and welcome to the Department of Chemistry at Johns
Hopkins University. As you will see throughout this brochure,
we offer an exciting environment for graduate studies in all areas
of the chemical sciences. Our department has a unique
advantage in its ability to maintain internationally recognized
research programs in a wide variety of chemical disciplines, while
remaining small enough for close student-faculty interactions. This
tradition of excellence has been carried forward from the department’s
inception as the first Ph. D. program in chemistry in America, and as you
will see, is now continued by an outstanding group of scientific leaders
that make up the Chemistry Department faculty. It is an exciting time to
enter our department. The Chemistry department resides in Remsen Hall,
which underwent a complete renovation in the 1990’s, Dunning Hall, and
the new state-of-the-art Chemistry building that is being constructed to
accommodate department growth. The building will follow a Georgian
style (see sketch) to blend with the Hopkins campus. Students choosing to
do their graduate work here will benefit from cutting-edge research
programs and facilities, while working in a friendly environment in which
access to faculty is unrestricted.
Students can work on many projects that cross the traditional
lines of chemistry, ranging from materials chemistry and surface
science to bioorganic and bioinorganic chemistry. There is an
extraordinary commitment here by the faculty towards the
development and growth of the graduate students; one only has to
look at the many students who have graduated from the Chemistry
Department and gone on to successful careers in both industry and
academia as concrete evidence of this commitment.
The Department is located on the Homewood campus of Johns
Hopkins University, approximately 3 miles from the Inner Harbor
of downtown Baltimore. The city of Baltimore offers all of the
advantages and recreational activities of a major metropolitan area,
and has seen a fantastic revitalization in the downtown section and
Inner Harbor in the past few years. Many other outstanding
research institutions are located in the Baltimore/Washington D.C.
area, including the National Institutes of Health (NIH) in Bethesda,
Maryland, the National Institute of Standards and Technology (NIST) in
Gaithersburg, Maryland, the Food and Drug Administration (FDA), the
National Aeronautics and Space Administration (NASA), the Naval
Research Laboratory (NRL), the Army Research Laboratory (ARL), and
the University of Maryland’s Baltimore County campus, as well as its
Biotechnology Institute at College Park. This concentration of scientific
research centers and programs is one of the highest in the country and
gives students in the Chemistry Department the opportunity for
collaborations and other interactions, including seminars and meetings
with different scientists from private industry, government laboratories
and other academic institutions. If you are interested in this type of
stimulating environment and are committed to pushing the boundaries of
the scientific frontier, we invite you to join one of the country’s
outstanding chemistry departments.
2 Graduate Study in Chemistry at The Johns Hopkins University

Baltimore
Johns Hopkins University is located within the city
of Baltimore, a very livable and affordable East
Coast city situated between Philadelphia and
Washington. The Chemistry Department is housed
on the Homewood campus, which lies within a
residential neighborhood about 2 miles north of the
central business area.
Baltimore has undergone an urban renaissance in
recent years. Many long established neighborhoods have
experienced a significant influx of new residents. The
area around the Homewood Campus continues to be an
attractive neighborhood in which to live, and is
typified by artistic brownstones, row houses, and newer
apartment buildings.
The city offers ample recreational and cultural activities.
Harborplace, located along the scenic Inner Harbor just south of the
central business district, is a striking collection of pavilions and
promenades set at the water’s edge. The National Aquarium adjoins
Harborplace on the east and has undergone a major recent expansion. To
the south of Harborplace is the Maryland Science Center, which features a
variety of scientific exhibits and houses a planetarium and Imax theater.
To the west is the Camden Yards baseball stadium, home of the Baltimore
Orioles, and Raven’s Stadium, home of the Baltimore Ravens.
There are a number of major museums located within the city.
These include the Walters Art Museum, which possesses a large collection
of antiquities, and the Baltimore Museum of Art, which houses an
excellent collection of French Impressionist painting and is adjacent to the
Hopkins Homewood campus. Also located in the city is the Baltimore and
Ohio Railroad Museum, which has an extensive collection of historic
railway equipment, the Babe Ruth Museum, and a museum dedicated to
Edgar Allen Poe (a former Baltimore resident). Baltimore is also home to
several fine musical organizations. The Baltimore Symphony Orchestra is
world-renowned and offers a range of symphonic and “pop” music at the
modern Joseph A. Meyerhoff concert hall. The Baltimore Opera Company
performs at the renovated Lyric Theatre.
Throughout the year, a variety of festivals and special events occur
in Baltimore. These include the Preakness, which is held at Pimlico Race
course and is the second leg of thoroughbred racing’s Triple Crown, the
Baltimore Marathon, and Artscape, a citywide arts festival.
Baltimore is conveniently located to other
attractions in the mid-Atlantic region. Washington, D.C.
is less than an hour to the south by car or train and offers
some of the best museums and cultural offerings in the
country. Philadelphia is less than two hours north of
Baltimore. Within Maryland, the Chesapeake Bay and
the Atlantic shore offer water and beach
activities, while the mountains lie two hours west of
Baltimore, for skiing in the winter and year-round hiking
and camping.
Graduate Study in
Chemistry at The Johns Hopkins University
3

Johns Hopkins University
Establishment
Johns Hopkins University was the first American institution to offer and
emphasize graduate education. Its history began in 1867, when at the
request of Johns Hopkins, a successful Baltimore businessman, two
corporations were formed: Johns Hopkins University and Johns Hopkins
Hospital.
With this unique vision and generous private endowment, Daniel
Coit Gilman opened the doors to Johns Hopkins University in 1876.
Throughout the years, the name Johns Hopkins has become world
renowned and synonymous with scholarly excellence, cutting edge
scientific research, the advancement of medicine and care of humanity.
Johns Hopkins has consistently ranked among the top universities by U.S.
News and World Report.
Organization
Johns Hopkins University is a privately endowed, coeducational
institution consisting of several academic divisions. The Zanvyl Krieger
School of Arts and Sciences (which includes the Chemistry department)
and the G.W.C. Whiting School of Engineering occupy the Homewood
campus, a 200 year old estate located in a pleasant residential
neighborhood in northern Baltimore. The School of Medicine
and the School of Public Health and Hygiene are located in east
Baltimore adjacent to the Johns Hopkins Hospital. A regular 20
minute shuttle bus service connects the two campuses. The
Peabody Conservatory of Music is located in the elegant Mt.
Vernon neighborhood of Baltimore, between the two main
campuses and is also served by shuttle bus.
Also on the Homewood campus are the Space Telescope
Science Institute, which is the ground base for NASA’s Hubble
Space Telescope, and the Carnegie Institution of Washington, a
well known molecular biology research institute. The Applied
Physics Laboratory is located midway between Baltimore and
Washington, and the School of Advanced International Studies is
in Washington, D.C.
Johns Hopkins now has an
international identity with learning
centers in Italy and China, but
the city of Baltimore, and the
Homewood campus, remains its
home. No matter the season, this
incomparable campus consisting
of impeccable landscaping, marble
and iron balustrades, and red
brick halls, creates an air of
Victorian decorum. Whatever the
scholarly spirit, this campus
inspires!
4
Graduate Study in
Chemistry at The Johns Hopkins University

The Department of Chemistry
The Graduate Program
Financial Support
Each graduate student is provided with financial
support in the form of full tuition and a stipend,
assuming that normal progress toward the degree is
maintained. Financial support is provided from a
combination of teaching and research
assistantships. In addition to the regular stipend,
the department awards a number of fellowships
(Marks Awards) to students of exemplary promise.
Students are also encouraged to apply for the many
national fellowships that are available.
Course Requirements
Eight graduate-level courses are required, and a
program is tailored to the individual interests and
needs of each student during an advising session
with a faculty committee. Course requirements are
typically completed in the first year of graduate
study. Graduate courses can be taken within the
Chemistry Department or in other departments,
and a current list of possible courses can be found
on the Chemistry department’s web page
(www.jhu.edu/~chem). Many students take
selected courses in the Departments of Biology,
Biophysics, Earth and Planetary Sciences, Electrical
and Computer Engineering, Geography and
Environmental Engineering, Materials Science and
Engineering, Physics and Astronomy, as well as
Pharmacology and Molecular Sciences on the
Medical School campus.
Selecting a Faculty Advisor
The choice of a research advisor and dissertation
topic occurs during the first semester. To aid in this
process, new graduate students at Johns Hopkins
attend a series of research seminars given by
individual faculty members detailing their
current research activities. New graduate students
also meet individually with potential faculty
mentors. Most students join a research group and
begin their independent graduate work by the end
of the fall semester.
Oral Examination
To be recommended for candidacy for the Ph. D.
degree in Chemistry, each student must prepare and
defend a research proposal that describes his or her
objectives in the planned dissertation research. This
proposal should describe progress and accomplishments
to date and plans for future research. The
proposal is presented in writing to a faculty
committee two weeks before the scheduled oral
examination. The faculty committee consists of
three members of the Chemistry faculty; these faculty
should also be considered as a resource for the
student during the remainder of his/her studies.
Students are also required to pass a universityrequired
Graduate Board oral examination, for
which a committee of five Chemistry and outside
faculty members are assembled.
Research
Research is at the heart of the Ph.D. program at
Johns Hopkins, and descriptions of faculty member’s
research interests are contained in this
brochure. Throughout the graduate program,
coursework, seminars and presentations are
designed to help students with their research
activities and to prepare them for describing their
work to a scientific audience. For each graduate
student, the successful completion, publication and
dissemination of results from one or more research
projects forms the basis of the Ph. D. degree.
Dissertation and Defense
The final step towards a Ph.D. degree is the writing
of a thesis that describes a student’s independent
and original research accomplishments. This
dissertation is written in close consultation with
your faculty advisor. Finally, each student presents
his or her graduate research in a departmental
seminar and private defense before their
dissertation committee.
Graduate Study in
Chemistry at The Johns Hopkins University
5

The Department of Chemistry
Faculty Research
The Department of
Chemistry at Johns
Hopkins University is
made up of a diverse
group of faculty. In addition
to the traditional
areas of chemical
research, many interdisciplinary
research interests
are present within
the department, at the
interface of chemistry and fields including biology,
medicine, physics, and environmental and material
sciences. Each faculty member has included a brief
description of their research interests in this
brochure.
Several faculty members have joint
appointments with other departments including
Biology, Biophysics, Materials Science and
Engineering, and Pharmacology and Molecular
Sciences. A number of interdisciplinary programs
and research centers based at Johns Hopkins
include members of the Chemistry department.
These include the Materials Research Science and
Engineering Center on nanostructures with
enhanced magneto-electronic properties, the NSFsupported
environmental research program in
Redox-Mediated Dehalogenation Chemistry, and
the Program in Molecular Biophysics.
Remsen Lecture
Each year, the Department of Chemistry, in
collaboration with the Maryland Section of the
American Chemical Society, bestows a Remsen
Award to a noteworthy Chemist of international
acclaim. The award ceremony is accompanied by a
lecture given by the award recipient. The annual
Remsen Award Lectures were inaugurated in May,
1946 by the Maryland Section of the American
Chemical Society to honor Ira Remsen, Professor of
Chemistry and President of the Johns Hopkins
University. The Remsen Memorial Lecturers are
chemists of outstanding achievement, in keeping
with Ira Remsen’s long and devoted career as an
exponent of the highest standards in
teaching and research in chemistry.
Past Remsen Award Recipients include:
2001 Dr. Ad Bax NIH
2000 Dr. Alexander Pines UC-Berkeley
1999 Dr. Thomas J. Meyer UNC-Chapel Hill
1998 Dr. Peter B. Dervan Cal Tech
1997 Dr. William H. Miller UC-Berkeley
1996 Dr. David A. Evans Harvard University
1995 Dr. Alfred G. Redfield Brandeis University
1994 Dr. Edward I. Solomon Stanford University
1993 Dr. Christopher T. Walsh Harvard Medical School
1992 Dr. William Klemperer Harvard University
1991 Dr. Rudolph A. Marcus Cal Tech
Application and Admission
No formal degree is required for admission, although entering students usually hold a
bachelor’s or master’s degree in chemistry or a related science. All applicants for admission are required to
furnish academic transcripts, three letters of recommendation, and scores of Graduate Record
Examinations, including the Advanced Chemistry Examination. An application to our graduate program is
included at the end of this brochure and on our web page (www.jhu.edu/~chem).
For further information, or if you have any questions, please contact:
Academic Program Coordinator
Phone: 410-516-7427
Fax: 410-516-8420
E-mail chem.grad.adm@jhu.edu
Faculty members are also happy to answer questions about their individual research interests; their e-mail
addresses are included in the faculty research section of this brochure.
6
Graduate Study in
Chemistry at The Johns Hopkins University

Kit H. Bowen
Experimental Physical Chemistry: Clusters and Nanoparticles
kitbowen@jhu.edu
Clusters are aggregates of atoms and/or molecules held together by the same
interatomic or intermolecular forces which are responsible for cohesion in
solids and liquids. Clusters are thus finite-size microcosms of the condensed
phase, the realm in which most chemistry occurs. A major objective of Dr.
Bowen’s research is to provide a molecule’s eye view of many-body, condensed
phase interactions. The study of size-specific and composition-specific clusters
provides an incisive means of addressing this fundamental and longstanding problem
in phyical chemistry.
For technical reasons, clusters are best studied as negatively-charged species.
Experimental methods utilized in Dr. Bowen’s group to study clusters include both
continuous and pulsed negative ion photoelectron spectroscopy, mass spectrometry,
and photodissociation spectroscopy. This work is instrumentally oriented, with major
components of his several ion beam apparatus including both continuous and pulsed
lasers, high vacuum systems, ion and electron optics, electronics and computers, as
well as time-of-flight, quadrupole, magnetic sector, and Wien filter mass
spectrometers. The training in advanced instrumentation, afforded students in Dr.
Bowen’s group, lays a firm foundation for careers in either physical or analytical
chemistry. Experimental emphasis is also placed on designing unique sources of
cluster ions and on the preparation and characterization of nanoparticles for a variety
of technological applications, such as catalysis.
A particularly attractive aspect of cluster studies concerns the very wide
variety of scientific problems that can be addressed, stretching from the edge of
biology, through chemistry and condensed matter physics, to the edge of
astrophysics. Using the versatile techniques described above, Dr. Bowen’s group is
studying the number of water molecules necessary to induce the formation
of zwitterions in amino acids, the energetics of electron capture in
hydrated nucleic acid bases, the solvent-induced stabilization of otherwise unstable
organic anions, the solvation of anions by aqueous and non-aqueous solvents, the
energetics and growth paths of charged atmospheric aerosols, the microscopic
conditions necessary for forming solvated electrons, the stability of color centers in
nanocrystals of metal compounds, the insulator-to-metal transition in clusters of
divalent metals, the electronic structure of alkali metal clusters, the prospects for
magic clusters as building blocks of futuristic cluster-assembled materials, the nature
of exotic species such as dipole bound and double Rydberg anions, the magnetism
exhibited by silicon-encapsulated transition metals, and the role of nanoclusters in
interstellar dust. The opportunity to be involved in such a diversity of fields is an
exciting aspect of this work for Dr. Bowen and his research group.
Ph.D., Harvard University
Postdoctoral, Harvard
University
Fellow, American Physical
Society
Humboldt Research Awardee
K + K + K + K +
Selected Publications include:
“In search of theoretically-predicted magic clusters: lithium-doped aluminum cluster anions,” O.C. Thomas, W.-J. Zheng, T.P. Lippa,
S.-J. Xu, S.A. Lyapustina, and K.H. Bowen, J. Chem. Phys. 114, 9895 (2001).
“Solvent-induced stabilization of the naphthalene anion by water molecules: A negative cluster ion photoelectron spectroscopic
study”, S.A. Lyapustina, S.-J. Xu, J.M. Nilles, and K.H. Bowen, J. Chem. Phys. 112, 6643 (2000).
“Vibrationally-resolved photoelectron spectroscopy of MgO - , and ZnO - , and the low-lying electronic states of MgO, MgO - , and
ZnO”, J.H. Kim, X. Li, L.-S. Wang, H.L. deClercq, C.A. Fancher, O.C. Thomas, and K.H. Bowen, J. Phys. Chem. A. 105, 5709
(2001).
K +
Al - 13
K + K +
K + 7
“Magic numbers in copper-doped aluminum cluster anions”, O.C. Thomas, W.–J. Zheng, and K.H. Bowen, J. Chem. Phys. 114,
5514 (2001).
The cluster-assembled ionic
“molecule”, KAl 13 , the kernel of
a new material
Graduate Study in
Chemistry at The Johns Hopkins University

Paul J. Dagdigian
Experimental Physical Chemistry
Gas-Phase Collision Dynamics and Spectroscopy
pjdagdigian@jhu.edu
Ph. D., University of
Chicago
Postdoctoral, Columbia
University
Fellow, American Physical
Society
We are employing laser fluorescence excitation and resonance-enhanced
multiphoton ionization of atoms and small molecules in studies of
gas-phase collisional processes, involving chemical reactions,
photodissociation, and nonreactive energy transfer processes. Recent
work has included the study of collision-induced rotational and
electronic transitions in the CN radical and the photodissociation of vibrationally
excited methyl chloride.
We are also interested in understanding the non-bonding interactions
between light atoms, such as boron, carbon, aluminum, and silicon, with rare gases
and small molecules such as H 2 . We interrogate these interactions through the
measurement of the electronic spectra of weakly bound complexes of these species,
prepared in a free-jet supersonic expansion. Such studies allow us to infer the
evolution of the chromophore of an atomic transition from that in the free atom,
binary and higher complexes through to the atom-doped solid.
There is a continuing need for the development of laser diagnostics for the
detection of transient species in reactive environments, as well as the detection of
explosives in trace quantities. Our group is participating in a recently funded DoD
multi-university initiative, “Spectroscopic and Time Domain Detection of Trace
Explosives in Condensed and Vapor Phases.” We will be implementing cavity
ring-down spectroscopy (CRDS) as one of a suite of ultrasensitive laser analytical
techniques to be applied to the detection of land mines. In our laboratory, we are also
employing CRDS to study the spectroscopy and kinetics of transient intermediates,
for example the H 2 CN radical.
Selected Publications include:
Tan, X.; Dagdigian, P. J.; and Alexander, M. H., “Electronic Spectroscopy and Excited State Dynamics of the Al–H 2 /D 2 Complex,”
Faraday Discuss. 2001, 118, 387.
Lei, J.; and Dagdigian, P. J., “Laser Fluorescence Excitation Spectroscopy of the CAr van der Waals Complex,” J. Chem. Phys.
2000, 113, 602.
Lei, J.; Teslja, A.; Nizamov, B.; and Dagdigian, P. J., “Free-Jet Electronic Spectroscopy of the PO 2 Radical,” J. Phys. Chem. A 2001,
105, 7828.
Nizamov, B.; Dagdigian, P. J.; and Alexander, M. H., “State-Resolved Rotationally Inelastic Collisions of Highly Rotationally Excited
CN(A 2 ∏) with Helium: Influence of the Interaction Potential,” J. Chem. Phys. 2001, 115, 8393.
8 Graduate Study in Chemistry at The Johns Hopkins University

David E. Draper
Physical Biochemistry
draper@jhu.edu
“
RNA folding” has become a vigorous area of research as many unexpected and
important functional roles have been discovered for RNA molecules. Research
in my lab is concerned with two related questions about RNA: What are the
energetics of folding compact RNA tertiary structures How do proteins
recognize specific RNA sites and carry out specific tasks A variety of
physical, biochemical, and genetic techniques are being used to explore several RNA
systems.
For a number of years, we have used ribosomal protein - RNA complexes as
systems to explore different aspects of protein - RNA recognition and RNA folding.
Most of our current efforts in this area concern two highly conserved regions of the
ribosome that bind elongation factor G (EF-G), which catalyzes GTP hydrolysis and
translocation of the ribosome along the messenger RNA. Each region consists of a
ribosomal RNA fragment and several ribosomal proteins; assembly of these
complexes and their interactions with EF-G are being studied by physical methods.
Mutations whose properties are known from the in vitro studies are being introduced
into ribosomes in vivo, to probe the functional significance of the complexes that are
being prepared. Initial work in this area resulted in the first crystal structure of a
ribosomal protein - RNA complex (Conn et al., 1999), which, in conjunction with
solution thermodynamic studies, has yielded considerable insight into protein - RNA
recognition mechanisms and unexpected features of RNA tertiary folding. Our
crystallographic efforts are being carried out in collaboration with Prof. Ed Lattman’s
laboratory in the Biophysics Department.
In the last few years we have been particularly concerned with electrostatic
aspects of RNA. Folding of an RNA tertiary structure is opposed by the unfavorable
free energy needed to bring negatively charged phosphates into proximity, and it has
long been known that Mg 2+ is much more effective than monovalent ions at
reducing the electrostatic free energy of RNA tertiary folds. We have recently
developed a theoretical framework for describing cation interactions with RNA. The
model successfully accounts for the special properties of Mg 2+ , and we are making
direct experimental measurements of Mg 2+ - RNA interactions to further test our
predictions. In other work, we are examining the electrostatic component of protein -
RNA binding, and again are making measurements in simple peptide - RNA
complexes to test our theoretical predictions quantitatively.
Ph.D., University of
Oregon
Postdoctoral, University
of Colorado
NIH Career Development
Award
NIH MERIT Award
Selected publications include:
Conn, G. L., Gittis, A. G., Minod, V., Lattman, E. E. & Draper, D. E. (2002). A compact RNA tertiary structure contains a buried
backbone - K + complex. J. Mol. Biol., 318, 963-973.
Misra, V. K. & Draper, D. E. (2001). A thermodynamic framework for Mg 2+ binding to RNA. Proc. Natl. Acad. Sci. U S A 98, 12456-
12461.
Misra, V. K. & Draper, D. E. (2002). The linkage between magnesium binding and RNA folding. J. Mol. Biol., 317, 507-521.
Gerstner, R. B., Pak, Y. & Draper, D. E. (2002). Recognition of 16S rRna by ribosomal protein S4 from Baccillus stearothermophilus.
Biochemistry 40, 7165-7133.
Shiman, R. & Draper, D. E. (2000). Stabilization of RNA tertiary structure by monovalent cations. J. Mol. Biol., 302, 79-91.
Draper, D. E. (1999). Themes in RNA-protein recognition. J. Mol. Biol., 293, 255-270.
Conn, G. L., Draper, D. E., Lattman, E. E. & Gittis, A. G. (1999). Crystal structure of a conserved ribosomal protein - RNA complex.
Science, 284, 1171-1174.
Graduate Study in
Chemistry at The Johns Hopkins University
9

D. Howard Fairbrother
Ph.D., Northwestern
University
Postdoctoral, University
of California, Berkeley
NSF CAREER Award
Experimental Surface Chemistry
Reactions at Polymer and Environmental Interfaces
Materials Processing
howardf@jhu.edu
Dr. Fairbrother’s research program is focused on elucidating the mechanisms of
chemical reactions that occur on surfaces and in thin films as well as their
impact on material properties. This interest is motivated by the wide range of
technologically significant processes that are mediated by surface reactions
including catalysis, materials processing as well as adhesion and friction.
The modification of polymer surfaces in vacuum environments is important
in a number of different situations including plasma processing, polymer
metallization and for vehicles in low earth orbits. We are exploring the microscopic
surface events that accompany polymer surface processing (Figure 1) and their impact
on interfacial properties. For example, we have explored the modification of
fluorinated organic films during X-ray irradiation and metallization as well as the
reactions of oxygen free radicals with self assembled monolayers.
Surface reactions are also responsible for a wide range of environmental
processes including atmospheric chemistry on ice and aerosol particles and the
elementary reaction steps in Fe-based organohalide remediation in groundwater.
Using an electrochemical cell coupled to a surface analysis chamber we are studying
the liquid/solid interface, specifically the effect of surface composition on the rate and
product partitioning associated with Fe-based organohalide remediation. In related
studies we are also studying the mechanisms associated with electron beam and
plasma remediation of chlorocarbons in aqueous solutions (Figure 2).
Our studies utilize a wide variety of modern surface analytical tools
including X-ray Photoelectron Spectroscopy (XPS), Infrared Spectroscopy, Mass
Spectrometry and Atomic Force Microscopy (AFM). A number of our projects are
highly collaborative in nature, involving interactions with the Department of
Geography and Environmental Engineering and the Department of Materials Science
and Engineering.
Selected Publications:
“Electron-Stimulated Chemical Reactions in Carbon Tetrachloride/Water (Ice) Films” A. J. Wagner, C. Vecitis, D. H. Fairbrother,
J. Phys. Chem. B. 102 (2002) 4432.
“Effect of X-ray Irradiation on the Chemical and Physical Properties of Semifluorinated Self- Assembled Monolayer”, A. J. Wagner,
S. R. Carlo, C. Vecitis, D. H. Fairbrother, Langmuir 18 (2002) 1542.
“Self-Assembled Monolayers as Models for Polymeric Interfaces,” C. C. Perry, S. R. Carlo, A.
J. Wagner, C. Vecitis, J. Torres, K. Kolegraf, D. H. Fairbrother (ACS Symposium Series on “Solid Surfaces and Thin Films”)
“Radical Reactions with Organic Thin Films: Chemical Interaction of Atomic Oxygen with an X-ray Modified Self-Assembled
Monolayer” J. Torres, C.C. Perry, S.J. Bransfield, D.H. Fairbrother, J. Phys. Chem. B., 106 (2002) 6265.
Figure 1: AFM image of a PTFE
(Teflon) surface during Ti
Deposition
Figure 2: Mass Spectrum of Volatile Species Produced
during Electron Beam Irradiation of Ice (bottom)
and a 13 CCl 4 /Ice Film (top)
10 Graduate Study in Chemistry at The Johns Hopkins University

David P. Goldberg
Inorganic Chemistry
Bioinorganic Chemistry
Environmental Chemistry
dpg@jhu.edu
Our research addresses a number of interesting challenges in
inorganic/bioinorganic chemistry. Currently, our group is divided into two
main areas. Part of our research group is interested in the synthesis, physical
properties and reactivity of new porphyrinoid compounds. We have
recently discovered a method for synthesizing corrolazines, a new class of
porphyrin-like compounds that are related to ring-contracted compounds called
corroles. Corroles, known for over 30 years, have a remarkable advantage over
porphyrins in stabilizing high-valent oxidation states (e.g. Mn V , Fe IV , Co IV , Ni III ), yet
little is known about their ability to function as catalysts and/or mimics for
biological systems because of the difficulties encountered in their preparation. We
have synthesized Co, Ni, Cu, Mn, and Fe corrolazines, and are now mapping out a
new area of metallocorrolazine reactivity and catalysis. Applications immediately
envisioned for these complexes include their reactivity toward O 2 and H 2 O 2 for
oxygen activation, the oxygenation/functionalization of substrates such as
hydrocarbons, and their use in mediating the dehalogenation of environmentally
significant organohalides.
In another area, we are designing and synthesizing small-molecule analogues
of the active sites of certain metalloproteins. Many biological processes rely on
transition metals to effect catalytic reactions. For example, peptide deformylase (PDF)
relies on an unusual (His) 2 (Cys)Fe II (OH 2 ) active site for deformylation during
bacterial protein synthesis. We have synthesized new N 2 S thiolate ligands to mimic the
His 2 Cys coordination sphere found in PDF, and have prepared a family of new
transition metal complexes with these ligands. Some of these complexes represent
stabilized forms of intermediates postulated to exist during catalysis, such as
[(PATH)Zn(formate)], which was prepared from the useful synthon [(PATH)Zn(Me)].
Other complexes exhibit the functional capacity to effect the hydrolysis of certain
substrates (e.g. esters), and these reactions are being examined through kinetic
studies. We have recently prepared new, more elaborate ligands with imidazole
donors and are exploring their transition metal chemistry, including dinuclear,
hydroxo-bridged zinc complexes that are relevant to enzymes that cleave DNA and
RNA. The study of these complexes will shed light on the fundamental role of metal
ions in the related biological systems, and may lead to the development of
industrially important catalysts and novel pharmaceutical agents.
Ph.D. Massachusetts
Institute of Technology
NIH Postdoctoral Fellow,
Northwestern University
NSF CAREER Award
Alfred P. Sloan Research
Fellowship
Recent publications include:
Chang, S.; Karambelkar, V. V.; di Targiani, R. C.; Goldberg D. P. “Model Complexes of the Active Site of Peptide Deformylase: A
New Family of Mononuclear N 2 S-M II Complexes,” Inorg. Chem., 2001, 40, 194-195.
Ramdhanie, B.; Stern, C. L.; Goldberg. D. P. “Synthesis of the First Corrolazine: A New Member of the Porphyrinoid Family” J. Am.
Chem. Soc., 2001, 123, 9447-9448.
Chang, S.; Sommer, R.; Rheingold, A.; Goldberg, D. P. “A Model Complex of a Possible Intermediate in the Mechanism of Action of
Peptide Deformylase: First Example of an N 2 SZn-formate Complex,” J. Chem. Soc., Chem. Commun., 2001, 2396-2397.
Chang, S.; Karambelkar, V. V.; Sommer, R.; Rheingold, A.; Goldberg, D. P. “New Monomeric Cobalt(II) and Zinc(II) Complexes of a
Mixed N,S(alkylthiolate) Ligand: Model Complexes of (His)(His)(Cys) Metalloprotein Active Sites,”Inorg. Chem. 2001, 41, 239-
248.
Graduate Study in
Chemistry at The Johns Hopkins University
11

Marc M. Greenberg
Organic and Bioorganic Chemistry
mgreenberg@jhu.edu
Ph.D., Yale University
American Cancer Society
Postdoctoral Fellow,
California Institute of
Technology
Alfred P. Sloan Research
Fellowship
As the carrier of genetic information, it is no surprise that DNA damage and
repair is important in aging and a variety of genetically based diseases, such
as cancer. However, modified nucleic acids are becoming increasingly
important as diagnostic tools and therapeutic agents. The pivotal roles of
DNA in chemistry and biology are interwoven. For instance, the reactivity of
DNA with reactive oxygen species determines the types of structural modifications
(lesions) formed. The interaction of lesions with repair and polymerase enzymes in
turn determines their biological effects. Identifying the location and level of DNA
lesions in the genome may assist the diagnosis and treatment approach of disease.
Our research group uses organic chemistry to address questions concerning
the reactivity, function, structure, and uses of nucleic acids. Examples of current
projects in our group are:
• determining how nucleic acids are oxidatively damaged by synthesizing molecules
(e.g 1) that enable us to independently generate reactive intermediates at defined
sites in DNA.
• elucidating the effects of specific DNA lesions (e.g. 2, 3) on the function of nucleic
acids, and their structural basis.
• the development of methods and applications for modified oligonucleotide
synthesis.
To bring these projects to fruition we synthesize novel molecules and study
their behavior using a variety of physicochemical, biochemical, and biological
techniques. Recent accomplishments by our research group in these areas include:
• the discovery of novel pathways for DNA damage that produce tandem lesions
(Scheme 1).
• the discovery of the first example of irreversible inhibition of DNA repair by a DNA
lesion (Scheme 2).
• the first synthesis of oligonucleotides containing formamidopyrimidine lesions (e.g.
Fapy•dG) and determination of their effects on DNA repair and polymerase
enzymes.
• the development of highly efficient, convergent methods for oligonucleotide
conjugate synthesis.
In addition to continuing these research projects, the above discoveries have
given rise to new projects in our group that include the development of novel
radiosensitizing agents and mechanism based inhibitors of DNA repair enzymes.
Selected publications include:
Fapy•dA Induces Nucleotide Misincorporation Translesionally by a DNA Polymerase. Delaney, M. O.; Wiederholt, C. J.; Greenberg,
M. M. Angew. Chem. Int. Ed. 2002, 41, 771.
Oxygen Dependent DNA Damage Amplification Involving 5,6-Dihydrothymidin-5-yl in a Structurally Minimal System. Tallman, K.
A.; Greenberg, M. M. J. Am. Chem. Soc. 2001, 123, 5181.
(3)
The 2-Deoxyribonolactone Lesion Produced in DNA by Neocarzinostatin and Other DNA Damaging Agents Forms Cross-Links with
the Base-Excision Repair Enzyme Endonuclease III. Hashimoto, M.; Greenberg, M. M.; Kow, Y. W.; Hwang, J.-T.; Cunningham, R. P.
J. Am. Chem. Soc. 2001, 123, 3161.
Introducing Structural Diversity in Oligonucleotides Via Photolabile, Convertible C5-Substituted Nucleotides. Kahl, J. D.; Greenberg,
M. M. J. Am. Chem. Soc. 1999, 121, 597.
Scheme 1 Scheme 2
1
2
12
Graduate Study in
Chemistry at The Johns Hopkins University

Bioorganic Chemistry and Enzymology
hendrick@jhu.edu
Tamara L. Hendrickson
Our research group is interested in evaluating the mechanisms and
consequences of complex enzymatic systems, within the broad field of
protein translation. We use a multidisciplinary approach, integrating tools
from biochemistry, molecular biology, enzymology and synthetic organic
chemistry.
Several projects focus on an indirect pathway for tRNA aminoacylation.
Traditionally, it was believed that all organisms use 20 aminoacyl-tRNA synthetases
(one for each encoded amino acid) to biosynthesize a complement of
aminoacyl-tRNAs. The wealth of genomic data that has become available over the
past few years, however, has revealed that many bacteria and archaea thrive in the
absence of glutaminyl- and/or asparaginyl-tRNA synthetase. In these cases,
tRNA Gln and tRNA Asn are misacylated respectively by either glutamyl- or
aspartyl-tRNA synthetase. Next, a glutamine-dependent amidotransferase
(Glu-AdT) converts the misacylated tRNA to the correct species. (Fig. 1 depicts this
process for the generation of glutaminylated-tRNA Gln .) Very little is known about
Glu-Adt, its mechanism of action or the methods by which it recognizes two different
tRNA substrates (tRNA Gln and tRNA Asn ). Several projects in our lab seek to address
some of these issues, by evaluating Glu-Adt from the stomach ulcer-inducing
pathogenic bacterium H. pylori, from human mitochondria and from the
hyperthermophilic archaeon P. furiousus.
The second area of interest in the lab is the biosynthesis of glycosyl
phosphatidylinositol (GPI) membrane anchored proteins (Fig. 2). GPI anchor
attachment converts a soluble protein into a membrane-associated protein. The
complexity of this system is due to the specificity with which a putative transamidase
(GPI-T) aligns two large substrates, targeting the carbohydrate anchor to a particular
amide bond within the protein substrate. GPI proteins are found throughout
eukaryotes, and are particularly abundant in some forms of parasitic protozoa,
making this modification a potential target for drug design. We are currently
developing the first soluble kinetic assay for GPI-T by synthetically incorporating
chromophoric groups into a typical peptide substrate. The development of such an
assay will enable the first detailed examination of the mechanism of action of this
complex enzyme.
Selected publications
Hendrickson, T. L., Nomanbhoy, T. K., de Crecy-Lagard, V., Schimmel, P. “Mutational Separation of Two Pathways for Editing by a
Class I tRNA Synthetase,” Mol. Cell, 2002, 9, 353-362.
Ph.D., California Institute
of Technology
NIH Postdoctoral Fellow,
Massachusetts Institute of
Technology and The
Scripps Research Institute
Research Corporation
Innovation Award
Hendrickson, T. L. “Recognizing the D-Loop of Transfer RNAs,” Proc. Natl. Acad. Sci., 2001, 98, 13473-13475.
Döring, V.; Mootz, H. D.; Nangle, L. A.; Hendrickson,T. L.; de Crécy-Lagard, V.; Schimmel, P.; and Marliére, P. “Enlarging the Amino
Acid Set of Escherichia coli by Infiltration of the Valine Coding Pathway,” 2001, 292, 501-504.
Hendrickson, T. L.; Spencer, J. R.; Kato, M.; Imperiali, B. “Design and Evaluation of Potent Inhibitors of Asparagine-Linked Protein
Glycosylation,” J. Am. Chem. Soc., 1996, 118, 7636-7637.
Graduate Study in
Chemistry at The Johns Hopkins University
13

Kenneth D. Karlin
Ph. D., Columbia
University
Postdoctoral, Cambridge
University, England
Editor, Progress in
Inorganic Chemistry
(Wiley)
Buck-Whitney Award
Biological and Environmental Inorganic Chemistry
Synthetic Models for Heme and/or Copper Proteins
Reactions with O 2 , NOx & R-Cl; Cu-DNA & peptide interactions
karlin@jhu.edu
Dr. Karlin’s bioinorganic research focuses on coordination chemistry relevant to
biological and environmental processes. Essential proteins with active-site
copper aggregates or heme (porphyrin-iron) centers react with O 2 or nitrogen
oxides. Thus, we study reactions involving O 2 , NO – 2 (nitrite), NO (nitric
oxide), N 2 O (nitrous oxide) as well as organohalides. Metal/O 2 chemistries
with organic substrates, DNA and proteins are also under investigation.
Our laboratory approaches include (a) the rational design and syntheses of
ligands allowing formation of appropriate Cu or Fe complexes, b) elucidation of
structure and physical properties using X-ray crystallography and a variety of
physical methods, and c) reactivity and kinetic-mechanistic investigations. The
studies should provide insights to questions of biological concern, and also may
provide a rationale for the chemist to design practical reagents for O 2 -mediated
oxidations, NOx-reduction catalysts, or agents which can dehalogenate R-Cl
pollutants.
Recent notable achievements (also see diagrams below) include: (a) the
detailed characterization of several types of copper-dioxygen adducts, including the
trans -1,2-peroxodicopper(II) complex shown below, (b) the generation of
cytochrome c oxidase (heme-copper) O 2- reactivity models, with -peroxo Fe III -(O 2
2–)
-Cu II and -oxo Fe III -(O 2– )-Cu II species, and (c) the demonstration that in a highly specific
manner, certain ligand-Cu 2 (or Cu 3 ) complexes oxidatively cleave DNA at the
junction of double and single-stranded regions.
Recent publications include:
Zhang, C. X.; Liang, H.-C.; Kim, E.-i.; Gan, Q.-F.; Tyeklár, Z.; Lam, M.; Rheingold, A. L.; Kaderli, S.; Zuberbühler, A. D.; Karlin, K. D.,
“Dioxygen Mediated oxo-transfer to an amine and oxidative N-dealkylation chemistry with a dinuclear copper complex”, Chem.
Commun., 2001, 631-632.
Ghiladi, R. A.; Hatwell, K. R.; Karlin, K. D.; Huang, H.-w.; Moënne-Loccoz, P.; Krebs, C.; Marzilli, L. A.; Cotter, R. J.; Kaderli, S.;
Zuberbühler, A. D. “Dioxygen Reactivity of Mononuclear Heme and Copper Components Yielding a High-Spin Heme-Peroxo-Cu
Complex”, J. Am. Chem. Soc., 2001, 123, 6183-6184.
Humphreys, K. J.; Karlin, K. D.; Rokita, S. E. “Recognition and Strand Scission at Junctions between Single- and Double-Stranded
DNA by a Trinuclear Copper Complex”, J. Am. Chem. Soc., 2001, 123, 5588-5589.
Fellow, American
Association for the
Advancement of Science
(AAAS)
Ira Remsen Chair
in Chemistry
14
Graduate Study in
Chemistry at The Johns Hopkins University

Thomas Lectka
Organic Chemistry
lectka@jhu.edu
The thrust of our research is towards the development of new catalytic
asymmetric reactions. In particular we are interested in chiral, all-organic
molecules, and Lewis acids as catalysts, as illustrated in three projects:
Project I. Catalytic, Asymmetric -Lactam and -Amino Acid Synthesis.
We have developed practical methodology for the catalytic, asymmetric synthesis
of lactams in high diastereo- and enantioselectivity employing chiral nucleophiles
as catalysts. Our reactions should provide access to a large number of serine protease
inhibitors of prostate specific antigen, cytomegalovirus protease, elastase, thrombin,
and cell metathesis. We have also recently developed a new synthesis of amino acid
derivatives through a catalytic, asymmetric process in which the chiral nucleophile
benzoylquinine (BQ) plays no less than five discrete roles. The reaction is a
multistage, multicomponent reaction in which the starting materials are inexpensive.
Project II. Asymmetric Catalysis on Sequentially-Linked Columns.
The all-organic nature of our catalyst systems renders them attractive to attach to a
solid phase. Along those lines, we have developed a catalytic, asymmetric process in
which reactions are conducted on a series of sequentially-linked columns packed with
solid-phase based catalysts and reagents. Our goal is ultimately to produce a
“synthesis machine” in which a complex series of transformations is conducted on the
column assemblies.
Project III. Catalytic, Asymmetric Halogenation.
The third project we have underway concerns the development of catalytic,
asymmetric halogenation reactions. Asymmetric halogenation represents a
challenging new frontier in asymmetric synthesis.
Representative Publications:
“Catalytic, Enantioselective Alkylation of Imino Esters: The Synthesis of Nonnatural Amino Acid Derivatives” J. Am. Chem.
Soc. 2002, 124, 67-77.
“Asymmetric Catalysis on Sequentially-Linked Columns” J. Am. Chem Soc. 2001, 123, 10853-10859.
“Reactive Ketenes through a Carbonate/Amine Shuttle Deprotonation Strategy: Catalytic, Enantioselective
Halides” Org. Lett. 2001, 3, 2049-2051.
“Catalytic, Asymmetric Halogenation” J. Am. Chem. Soc. 2001, 123, 1531-1532.
“Catalytic, Asymmetric Synthesis of Lactams” J. Am. Chem. Soc. 2000, 122, 7831-7832.
Bromination of Acid
Ph.D. Cornell University
Postdoctoral, Universität
Heidelberg
NIH Postdoctoral Fellow,
Harvard University
Alfred P. Sloan Research
Fellowship
Camille Dreyfus Teacher-
Scholar Award
DuPont ATE Award
NSF CAREER Award
Eli Lilly Young Investigator
Grantee
NIH First Award
Graduate Study in
Chemistry at The Johns Hopkins University
15

Gerald J. Meyer
Inorganic Materials Chemistry
Environmental Chemistry
meyer@jhu.edu
(a)
Ph.D., University of
Wisconsin at Madison
Postdoctoral, University
of North Carolina at
Chapel Hill
The Meyer group research focuses on inorganic chemistry with a particular
emphasis on the interface between molecules and solid-state materials. A
theme of our research has been to design materials at the molecular level that
have desired optical, electrical, environmental, biological, magnetic, and/or
catalytic functions. Summarized below are three key research areas:
We prepare solar cells, based on
Nanocrystalline Semiconductor Interfaces.
nanocrystalline semiconductors sensitized to light with inorganic coordination
compounds that efficiently convert sunlight into electrical power. These materials
also allow interfacial electron transfer processes to be quantified in unprecedented
molecular detail. Shown below, is a schematic representation of an interface designed
for fundamental photo-induced electron transfer studies. Other ongoing research
projects with these interfaces include the study of bimetallic compounds, charge
transport, energy transfer, and catalysis.
Magnetic Nanowire Interfaces. Nanowires with segments of different magnetic and
non-magnetic materials are prepared in our labs. An example is shown below where
a magnetic nickel segment has been functionalized with a fluorescent dye while a
non-magnetic gold segment has not. In the visible image (a) the two wire segments
appear similar while the fluorescent image (b) clearly reveals the nickel segment. The
magnetic properties of the nanowire materials are under active study as part of the
Hopkins’ NSF-funded MRSEC and can be used for applications in separations, sensing,
magnetic recording and biotechnology.
Environmental Interfaces. We prepare materials that convert sunlight into electrical
power and materials that can decontaminate water of halocarbon pollutants. This
latter project is the subject of a NSF-funded ‘CRAEMS’ program that involves
interdisciplinary research with five Hopkins groups. Our approach has been to study
mechanistic aspects of organohalide reaction with natural and synthetic iron
porphyrins. These studies provide insights into how living organisms can both
dehalogenate organic halocarbons and die from exposure to them.
Recent Publications:
Pseudo-halogens for Dye-Sensitized TiO 2 Photoelectrochemical Cells. Oskam, G.; Bergeron, B.V; Meyer, G.J.; Searson,
P.C. J. Phys. Chem. B 2001, 105, 6867.
Long Distance Electron Transfer Across Molecular-Nanocrystalline Semiconductor Interfaces. Galoppini, E.; Guo, W.;
Qu, P.; Meyer, G.J. J. Am. Chem. Soc. 2001, 123, 4342.
Magnetic Alignment of Fluorescent Nanowires. Tanase, M.; Bauer, L.A.; Hultgren, A.; Silevitch, D.M.; Sun, L.; Reich, D.H.;
Searson, P.C.; Meyer, G.J. NanoLett. 2001, 1, 155.
Proton Controlled Electron Injection from Molecular Excited States to the Empty States in Nanocrystalline TiO 2 .
Qu, P.; Meyer, G.J. Langmuir 2001, 17, 6720.
(b)
Crowded Cu(I) Complexes Involving Benzohquinoline: π-Stacking Effects and Long Lived Excited States. Riesgo,
E.C.; Hu, Y.-Z.; Bouvier, F.; Thummel, R.P.; Scaltrito, D.V.; Meyer, G.J. Inorg. Chem. 2001, 40, 3413-3422.
16
Graduate Study in
Chemistry at The Johns Hopkins University

Douglas Poland
Theoretical Chemistry
Statistical Mechanics, Kinetics of Cooperative Processes,
Distribution Functions in Proteins and Nucleic Acids
poland@jhu.edu
Early in my career I was interested in the application of the methods of
equilibrium statistical mechanics to the problem of conformational transitions
(helix-coil) transitions in proteins and nucleic acids. This work is reviewed in
two books: (with H.A. Scheraga) Theory of Helix-Coil Transitions in Biopolymers
(Academic Press, New York, 1970) and Cooperative Equilibria in Physical
Biochemistry (Oxford University Press, London, 1978). My interests then turned to
simple lattice-gas models for phase transitions. This work involved extensive
calculation of exact series expansions for thermodynamic functions for various latticegas
models and the analysis of the series (search for phase-transition singularities). I
also became interested in the use of statistical mechanics to treat the kinetics of
cooperative phenomena such as cooperative adsorption and enzyme reaction
networks. The general problem in this area of study is to understand the nonlinear
equations that arise in such systems. When a system is far from equilibrium
instabilities can arise, often giving rise to limit cycles (oscillations in the density) or
chaotic behavior.
Recently my interests have returned to biological macromolecules. In
particular I have been exploring ways to determine distributions functions for various
molecular properties. For example, given the temperature dependence of the heat
capacity one can convert this data into a finite set of moments of the distribution
funtion for molecular enthalpies (analog of the Maxwell-Boltzmann distribution of
kinetic energies). Given a set of moments one can then use the maximum-entropy
method to construct an approximate distribution function, the quality of the
approximation increasing with the number of moments used. For many proteins this
distribution function is bimodal, indicating the presence of two major species, the
native and denatured form of the protein. This same technique can be used to
determine distribution functions for the number of ligands bound to proteins and
nucleic acid using data from an appropriate binding isotherm.
Ph.D., Cornell University
Postdoctoral, Cornell
University
Selected Publications Include:
Poland, D. "Maximum-Entropy Calculation of Energy Distributions", Journal of Chemical Physics, 2000, 112, 4774-4784.
Poland, D. "Enthalpy Distributions in Proteins", Biopolymers, 2001, 58, 89-105.
Poland, D. "Protein-Binding Polynomials", Journal of Protein Chemistry, 2001, 20, 91-97.
Graduate Study in
Chemistry at The Johns Hopkins University
17

Gary H. Posner
Organic Chemistry; Medicinal Chemistry
ghp@jhu.edu
Professor Posner’s research deals generally with development of new synthetic
methods and asymmetric synthesis of natural products, with special emphasis
on design and synthesis of new compounds having beneficial effects on the
quality of human life (i.e., new medicinal agents). Recently, the Posner
research team has prepared a promising analog of vitamin D 3 for treatment of
the skin disease psoriasis, a promising analog of the Chinese medicine qinghaosu for
treatment of malaria, and some new isothiocyanates as promising lead compounds
for prevention of cancer.
Professor Posner is well known for his involvement with organocopper
chemistry as a researcher and writer. His original research publications and his two
review articles and one book on organocopper chemistry have helped to make this
area one of the fastest developing ones in modern synthetic organometallic chemistry.
Recent publications include:
Posner, G.H.; Northrop, J.; Paik, I.-K.; Borstnik, K.; Dolan, P.; Kensler, T.W.; Xie, S.; Shapiro, T. A., “New Chemical and Biological
Aspects of Artemisinin-Derived Trioxane Dimers,” Bioorg. Med. Chem. 2002, 10, 227-232.
Ph.D., Harvard University
Postdoctoral, University
of California, Berkeley
Johns Hopkins University
Distinguished Teaching
Award
Executive Editor,
Tetrahedron Reports
Gardezi, S.A.; Nguyen, C.; Malloy, P.J.; Feldman, D.; Posner, G. H.; Peleg, S., “A Rationale for Treatment of Hereditary Vitamin D
Resistant Rickets with Analogs of 1 -25-Dihydroxyvitamin D 3 ,” J. Biol. Chem. 2001, 276, 29148-29156.
Posner, G. H.; Jeon, H.B.; Parker, M.H.; Krasavin, M.; Paik, I.-K.; Shapiro, T. A., “Antimalarial Simplified 3-Aryltrioxanes: Synthesis
and Preclinical Efficacy/Toxicity Testing in Rodents,” J. Med. Chem., 2001, 44, 3054-3058.
Posner, G.H.; Crawford, K.R.; Peleg, S.; Welsh, J.E.; Romu, S.; Gewirtz, D.A.; Gupta, M.S.; Dolan, P.; Kensler, T.W., “A Non-Calcemic
Sulfone Version of The Vitamin D3 Analog Seocalcitol (EB 1089): Chemical Synthesis, Biological Evaluation, and Potency
Enhancement of the Anticancer Drug Adriamycin,” Bioorg. Med. Chem., 2001, 9, 2365-2371.
Somjen, D.; Waisman, A.; Lee, J.K.; Posner, G.H.; Kaye, A.M., “A Noncalcemic Analog of 1,25-Dihydroxyvitamin D 3 (JKF)
Upregulates The Induction of Creatine Kinase B by 17-Beta-estradiol in Osteoblast-like ROS 17/2.8 Cells and in Rat Diaphysis,” J.
Steroid Biochem. Mol. Biol., 2001, 77, 205-212.
Szpilman, A.M.; Korshin, E.E.; Hoos, R.; Posner, G.H.; Bachi, M.D., “Iron(II)-Induced Cleavage of Antimalarial Beta-Sulfonyl
Endoperoxides. Evidence for the Generation of Potentially Cytotoxic Carbocations,” J. Org. Chem., 2001, 66, 6531-6540.
O’Neill, P.M.; Miller, A.; Bishop, L.P.D.; Hindley, S.; Maggs, J.L.; Ward, S.A.; Roberts, S.M.; Scheinman, F.; Hoos, R.; Posner, G.H.;
Park, B.K., “Synthesis, Antimalarial Activity, Biomimetic Iron(II) Chemistry, and the in vitro Metabolism of Novel, Potent C-10-
Phenoxy Derivatives of Dihydroartemisinin,” J. Med. Chem., 2001, 44, 58-68.
Guyton, K.Z.; Kensler, T.W.; Posner, G.H., “Cancer Chemoprotection Using Natural Vitamin D 3 and Synthetic Analogs,” Annu. Rev.
Pharm. Toxicol. 2001, 41, 421-442.
White, M.C.; Burke, M.; Peleg, S.; Bren, H.; Posner, G.H., “Conformationally Restricted Hybrid Analogs of the Hormone 1,25-
Dihydroxyvitamin D 3 : Design, Synthesis, and Biological Evaluation,” Bioorg. Med. Chem., 2001, 9, 1691-1699.
Posner, G.H.; Halford, B.; Dolan, P.; Kensler, T.W.; White, J.; Jones, G., “Conceptually New Low-Calcemic Oxime Analogs of the
Hormone 1-alpha, 25-Dihydroxyvitamin D3: Synthesis and Biological Testing,” J. Med. Chem., 2002, 45, 000.
Korshin, E.K.; Hoos, R.; Szpilman, A.M., Konstantinovski, L.; Posner, G.H.; Bachi, M.D., “An Efficient Synthesis of Bridged-Bicyclic
Peroxides Structurally Related to Antimalarial Yingzhaosu A based on Homolytic Co-Oxidation of Thiols and Monoterpenes,”
Tetrahedon, 2002, 58, 2449-2469.
18
Graduate Study in
Chemistry at The Johns Hopkins University

Harris J. Silverstone
Theoretical Chemistry
hjsilverstone@jhu.edu
My main research interests are quantum problems that cannot be solved in
simple closed form, but that can be solved by infinite series expansions,
especially divergent asymptotic expansions. Atoms in external electric and
magnetic fields are prime examples. When the external field is regarded as
a perturbation, the resulting series are asymptotically divergent.
Divergent series are interesting when they are “summable.” That is, when
there is a procedure for finding directly from the series the mathematical function that
the series represents. There is often a related, sometimes physical, quantity that is
“exponentially small” and that governs the rate of divergence of the series. In the case
of the electric field, the exponentially small quantity is the ionization rate. A new
development is a higher-order summation technique called hyperasymptotics that
uses the exponentially small subseries to sum the divergent series. The exponentially
small subseries are intimately connected with the “connection formula” problem in
semiclassical methods in quantum mechanics, such as the JWKB method.
The hyperasymptotics research is in collaboration with Professor Gabriel
Álvarez of the Departamento de Física Téorica II, Universidad Complutense,
Madrid, Spain, and with Professor Christopher J. Howls of the Faculty of
Mathematical Studies, University of Southampton, UK.
Research now complete provided a detailed feature-by-feature analysis of the
photoionization cross section of hydrogen in an electric field in terms of expansions
over resonances. Extension of the expansion to infinite fields led to a complete
understanding of the “Bender-Wu” branch cuts of the anharmonic oscillator, a
somewhat serendipitous result. Earlier work used perturbation expansions to
elucidate the transition between classical, semiclassical and quantum mechanics. Still
earlier work concerned electron correlation (how electrons avoid each other) in atoms
and molecules, the evaluation of molecular integrals using expansions generated from
Fourier-transforms, and the use of piecewise-polynomial expansions for electronic
wave functions.
A separate research interest, in collaboration with Professor Betty Jean
Gaffney of the Department of Biological Science, Florida State University, has been the
simulation of electron magnetic resonance spectra for high-spin iron in heme proteins
and in enzymes.
Ph.D., California Institute
of Technology
NSF Postdoctoral Fellow,
Yale University
Alfred P. Sloan Research
Fellowship
Selected publications include:
Connection formula, hyperasymptotics, and Schrödinger eigenvalues: dispersive hyperasymptotics and the anharmonic oscillator;
Gabriel Álvarez, Christopher J. Howls, and Harris J. Silverstone in Toward the Exact WKB Analysis of Differential Equations, Linear or
Non-Linear, edited by Christopher J. Howls, Takahiro Kawai, and Yoshitsugu Takei (Kyoto University Press, Kyoto, 2000).
Large-field behavior of the LoSurdo-Stark resonances in atomic hydrogen; Gabriel Álvarez and Harris J. Silverstone;
Phys. Rev. A 50, 4679-4699 (1994).
Simulation methods for looping transitions; Betty J. Gaffney and Harris J. Silverstone; J. Magn. Reson. 134, 57-66 (1998).
Anharmonic oscillator discontinuity formulae up to second-exponentially-small order; Gabriel Álvarez, Christopher J. Howls, and
Harris J. Silverstone; J. Phys. A 35, 4003-4016 (2002).
Dispersive hyperasymptotics and the anharmonic oscillator; Gabriel Álvarez, Christopher J. Howls, and Harris J. Silverstone;
J. Phys. A 35, 4017-4042 (2002).
Graduate Study in
Chemistry at The Johns Hopkins University
19

Joel R. Tolman
Biophysical Chemistry
jtolman@jhu.edu
Ph.D., Yale University
Human Frontier
Postdoctoral Fellow,
University of Toronto
Postdoctoral, École
Polytechnique Fédérale de
Lausanne
Within the past two decades, Nuclear Magnetic Resonance spectroscopy
(NMR) has become a powerful technique for the study of
macromolecular structure and dynamics in the solution state. Research
in my lab will be concerned with both the development and application
of novel NMR techniques for studying the complex interactions that
underlie biological function. Of particular interest are studies of molecular dynamics,
the nature of intermolecular recognition and the quaternary organization of multidomain
protein systems.
The full repertoire of multidimensional NMR methodology will be employed
to study these problems, including spin relaxation, scalar coupling, NOE, and
hydrogen exchange experiments. However, the primary approach will be centered
around recently developed techniques for the measurement of Residual Dipolar
Couplings (RDCs) in macromolecules. These RDCs, which are normally averaged to
zero in solution, are made observable by introducing a very weak degree of alignment
of the biomolecule relative to the magnetic field. This alignment is typically achieved
by dissolving the protein or nucleic acid along with a suitable co-solute, such as
bacteriophage particles. The resulting RDCs are relatively easily measured and
represent an abundant source of highly precise information on the relative
orientations of different internuclear ‘bonds’ within the molecule. Intriguingly, RDCs
also exhibit sensitivity to molecular motions on the nsec-sec timescales, during which
many functionally important motions occur. These motional timescales have
traditionally been very difficult to access experimentally, and thus a major objective
will be to develop RDC-based techniques to enable the study of these motions.
One of the applications of these techniques will be to investigate the
quaternary organization of tetrameric ubiquitin. Tetramers of the protein ubiquitin
can assume a multi-faceted role in cellular signal-transduction mechanisms, which
depends on how they are linked together. A major goal will be to gain insights into
the nature of this important and versatile signal through studies of its solution state
conformations. In addition, efforts are ongoing to develop methodology for the
simultaneous determination of both the 3-dimensional structure and a detailed
description of the dynamics of a protein. A closely related objective is to develop the
capability of using NMR to rapidly determine the backbone fold of a protein to
moderate resolution, which would represent an important contribution to current
structural genomics initiatives.
Selected publications include:
Tolman, J.R., “Dipolar Couplings as a Probe of Molecular Dynamics and Structure in Solution,”
Curr. Opin. Struct. Biol. 2001, 11, 532-539.
Al-Hashimi, H.M.; Tolman, J.R.; Majumdar, A.; Gorin, A.; and Patel, D.J., “Determining
Stoichiometry in Homomultimeric Nucleic Acid Complexes Using Magnetic Field Induced Residual
Dipolar Couplings,” J. Am. Chem. Soc. 2001, 123, 5806-5807.
Tolman, J.R.; Al-Hashimi, H.M.; Kay, L.E.; and Prestegard, J.H., “Structural and Dynamic Analysis
of Residual Dipolar Coupling Data for Proteins,” J. Am. Chem. Soc. 2001, 123, 1416-1424.
Tolman, J.R.; Flanagan, J.M.; Kennedy, M.A.; and Prestegard, J.H., “NMR Evidence for Slow
Collective Motions in Cyanometmyoglobin,” Nature Struct. Biol. 1997, 4, 292-297.
20 Graduate Study in Chemistry at The Johns Hopkins University

Organic Chemistry; Photochemistry and Photobiology;
Characterization of Reactive Intermediates
jtoscano@jhu.edu
John P. Toscano
Most photochemical reactions take place through very short-lived
intermediates such as singlet or triplet excited states, radicals, carbenes,
nitrenes, and nitrenium ions. A thorough understanding of these
intermediates is not only of basic scientific concern, but also has direct
relevance to many critical issues in photochemistry and photobiology. The
Toscano group’s main research interests involve the application of time-resolved
spectroscopic techniques to the study of these intermediates with particular emphasis
on the use of newly developed methods in time-resolved infrared spectroscopy.
Nitric oxide (NO), a diatomic radical known previously as a noxious
environmental pollutant, is now known to be involved in a wide range of important
bioregulatory processes including neurotransmission, blood clotting, and blood
pressure control. In addition, macrophages have been shown to kill cancerous tumor
cells and intracellular parasites by releasing large amounts of NO. Deficiencies in
these processes caused by a poor endogenous supply of NO are often treatable with
NO-releasing drugs. Diazeniumdiolates (1) are an interesting class of such drugs
presently under development. Recent efforts to make diazeniumdiolates more
effective pharmaceuticals have concentrated on using derivatives of such compounds
to deliver NO specifically to a targeted site. Given the large number of biological
phenomena now known to be mediated by NO, such targeting will be critical to the
success of most medical applications.
We have begun to develop photochemical precursors to diazeniumdiolates
that can be used as effective and potentially selective NO-releasing agents. Since
initial experiments in other laboratories with classical photoprotecting groups (P)
gave unexpected and disappointing results, we are presently clarifying reaction
pathways so that more efficient phototriggered NO-releasing drugs can be rationally
designed. In addition, if diazeniumdiolates are to enjoy routine medical use, their
basic photochemistry must be understood so that phototoxicity issues may be
anticipated and avoided.
Recent Publications Include:
Toscano, J. P. “Structure and Reactivity of Organic Intermediates as Revealed by Time-Resolved IR Spectroscopy” Adv. Photochem.
2001, 26, 41-91.
Srinivasan, A.; Kebede, N.; Saavedra, J. E.; Nikolaitchik, A. V.; Brady, D. A.; Yourd, E.; Davies, K. M.; Keefer, L. K.; Toscano, J. P.
“Chemistry of the Diazeniumdiolates. 3. Photoreactivity” J. Am. Chem. Soc. 2001, 123, 5465-5472.
Srivastava, S.; Ruane, P. H.; Toscano, J. P.; Sullivan, M. B.; Cramer, C. J.; Chiapperino, D.; Reed, E. C.; Falvey, D. E. “Structures of
Reactive Nitrenium Ions: Time-Resolved Infrared Laser Flash Photolysis and Computational Studies of Substituted N-Methyl-N-aryl-
Nitrenium Ions” J. Am. Chem. Soc. 2000, 122, 8271-8278.
Wang, Y.; Toscano, J. P. “Time-resolved IR Studies of 4-Diazo-3-Isochromanone: Direct Kinetic Evidence for a Non-Carbene Route to
Ketene” J. Am. Chem. Soc. 2000, 122, 4512-4513.
Ph.D., Yale University
NIH Postdoctoral Fellow,
Ohio State University
Camille and Henry Dreyfus
New Faculty Award
NSF CAREER Award
Camille Dreyfus Teacher-
Scholar Award
Alfred P. Sloan Research
Fellowship
“Controlled Photochemical Release of Nitric Oxide from O 2 -Benzyl Substituted Diazeniumdiolates” Ruane, P.H.; Bushan, K.M.;
Pavlos, C.M.; D’Sa, R.A.; Toscano, J. P. J. Am. Chem. Soc. 2002, in press.
“Solvent Dependence of the 2-Napthyl (carbomethoxy)carbene Singlet-Triplet Energy Gap” Wang, Y.; Hadad, C.M.; Toscano, J. P.
J. Am. Chem. Soc. 2002, 124, 1761-1767.
O
R2N N
+ h
N
O
P
O
R2N N
+
N
O
+
P
H 2 O
pH 7.4
R 2 NH + 2 NO + OH P
Graduate Study in
Chemistry at The Johns Hopkins University
21

Craig A. Townsend
Bioorganic Chemistry
townsend@jhunix.hcf.jhu.edu
Research programs in Dr. Townsend’s group are broadly in the area of
bioorganic chemistry with specific interests in natural product biosynthesis,
the enzymology and molecular biology of secondary metabolism and
molecular medicine. Underlying these studies are interests in reaction
mechanism and synthesis, notably biomimetic synthesis, mechanistic
enzymology, protein structure and protein engineering, exploration of the genetic
organization and over-expression of biosynthetic enzymes, and the study of and the
design and synthesis of fatty acid synthase inhibitors leading to practical treatments
in cancer, tuberculosis and obesity.
Recent publications include:
Khaleeli, N.; Li, R.-F.; Townsend, C. A. “Origin of the -Lactam Carbons in Clavulanic Acid from an Unusual Thiamine Pyrophosphate-
Mediated Reaction,” J. Amer. Chem. Soc. 1999, 121, 9223-9224. [See ‘Perspectives’ article: Science 2000, 287, 818-819.]
Challis, G. L.; Ravel, J.; Townsend, C. A. “Predictive, Structure-Based Model of Amino Acid Recognition by Non-Ribosomal Peptide
Synthetase Adenylation Domains,” Chemistry & Biology 2000, 7, 211-224.
Ph.D., Yale University
Postdoctoral,
Eidgenössiche
Teschnische Hochschule
Alfred P. Sloan Research
Fellowship
Camille Dreyfus - Teacher
Scholar Award
Loftus, T. M.; Jaworsky D.; Frehywot, G. L.; Townsend, C. A.; Ronnett, G.; Lane, M. D.; Kuhajda, F. J. “Inhibitors of Fatty Acid
Synthase Induce Weight Loss: A Link Between Fatty Acid Synthesis and Feeding Behavior,” Science 2000, 288, 2379-2381.
Jones, P. B.; Parrish, N. M.; Houston, T. A.; Stapon, A. S.; Bansal, N. P.; Dick, J. D.; Townsend, C. A. “A New Class of Anti-
Tuberculosis Agents,” J. Med. Chem. 2000, 43, 3304-3314.
Li. R.-F.; Stapon, A.; Blanchfield, J. T.; Townsend, C. A. “Three Unusual Reactions Mediate Carbapenem and Carbapenam
Biosynthesis,” J. Amer. Chem. Soc. 2000, 122, 9296-9297.
Miller, M. T.; Bachmann, B. O.; Townsend, C. A.; Rosenzweig, A. C. “Stucture of ß-Lactam Synthetase Reveals How to Synthesize
Antibiotics Instead of Asparagine,” Nature Struct. Biol. 2001, 8, 684-689.
Udwary, D.W.; Casillas, L.K.; Townsend, C.A. “Synthesis of 11-Hydroxyl O-Methylsterigmatocystin and the Role of a Cytochrome P-
450 in the Final Step of Aflatoxin Biosynthesis,” J. Amer. Chem. Soc. 2002, 124, 5294-5303.
Maryland Chemist of the
Year (1992)
ACS Arthur C. Cope
Scholar Award
22
Graduate Study in
Chemistry at The Johns Hopkins University

David R. Yarkony
Theoretical Chemistry
yarkony@jhu.edu
According to the Born-Oppenheimer approximation nuclei move on a single
potential energy surface created by the faster moving electrons. This
approximation is at the heart of our description of most chemical processes.
From protein folding to tribology to catalysis the Born Oppenheimer
approximation rules. So why study nonadiabatic processes, processes in
which the Born-Oppenheimer approximation breaks down. The answer is simple in
the absence of nonadiabatic processes life on earth, as we know it would not exist.
Light harvesting, vision and essential upper atmospheric processes depend on
electronically nonadiabatic steps. Of course this has been known for decades. What
is unusual and exciting is that in the last 10 years our way of thinking about
electronically nonadiabatic processes has begun to change, and change dramatically.
The changing face of nonadiabatic chemistry is the consequence of a rethinking of the
role of surface intersections (conical intersections) of states of the same symmetry
these processes. Once little more than a theoretical curiosity today conical
intersections of two states of the same symmetry are now understood to be an
essential part of nonadiabatic processes. This change in paradigm can dramatically
change the predicted/expected rate of a nonadiabatic process. My research group has
helped lead this revolution. Over the last decade we have developed the tools for
studying conical intersections that define the state of the art in this area and as a result
have lead the way in advancing the computational description of this singular
consequence of the separation of nuclear and electronic time scales. More recently we
have attacked the problem of nonadiabatic processes involving heavy atoms in which
the spin-orbit interaction and Kramers’ degeneracy play an essential role. Our work
in this area has provided the first ever location of a conical intersection in a
polyatomic molecule based on ab initio wave functions with the spin-orbit interaction
included in the Hamiltonian.
We are currently building on our expertise in the description of the
electronic structure aspects of nonadiabatic processes by developing fully quantum
mechanical wave packet methods to quantify the role of conical intersections in
nonadiabatic dynamics.
In summary, nonadiabatic chemistry is an important field with a bright new
future and we expect to continue to play a leading role in this area.
Recent publications
Nuclear Dynamics near conical intersections in the adiabatic representation: I. The effects of local topography on interstate transition: David
R. Yarkony, J.Chem. Phys., 114, 2601-2613 (2001).
Ph.D., University of
California, Berkeley
Postdoctoral,
Massachusetts Institute of
Technology
Fellow, American Physical
Society
Alfred P. Sloan Research
Fellowship
Conical intersections: The New Conventional Wisdom – Feature Article, D. R. Yarkony, J. Phys. Chem. A 105, 6277-6293 (2001).
On the Effects of Spin-Orbit Coupling on Conical Intersection Seams in Molecules with an Odd
Number of Electrons. I: Locating the Seam; Spiridoula Matsika and David R. Yarkony, J. Chem.
Phys. 115, 2038-2050 (2001).
On the Effects of Spin-Orbit Coupling on Conical Intersection Seams in Molecules with an Odd
Number of Electrons. II: Characterizing the local topography of the seam; Spiridoula Matsika and
David R. Yarkony, J. Chem. Phys. 115,5066-5075, (2001).
Graduate Study in
Chemistry at The Johns Hopkins University
23

Instrumentation
The department is well equipped with instrumentation to perform
modern chemical research. Routine instrumentation is housed in
the Instruments Facility in Remsen Hall and is maintained by staff
within the department. In addition, there is a large variety of
custom-built equipment in individual research laboratories.
Our nuclear magnetic resonance facilities includes a 500 MHz
Varian Unity instrument with full three-channel, gradients capability, a
Varian 400 MHz spectrometer upgraded to a Unity console, and a 300
MHz Bruker AMX. The lower-field NMRs are used for more routine synthetic
chemistry applications, while the high-field NMR is primarily dedicated
to multi-dimensional analysis of proteins and nucleic acids. In
addition, the undergraduate instructional laboratories house a Varian
Mercury 200 MHz spectrometer that is also available for research use.
In a joint initiative by the Departments of Biology, Biophysics, and
Chemistry, the Krieger School of Arts and Sciences has commissioned the
development of a Nuclear Magnetic Resonance Center for the study of the
structure and dynamics of biological macromolecules. This facility will be
constructed in connection with the new chemistry building, at a site
bridging the chemistry and biology departments. The first instrument to
be housed in this facility, a 600 MHz spectrometer, has recently been
ordered.
In addition to the NMR initiative, the department has recently
received funding to establish a state of the art small molecule x-ray
diffraction facility. This staffed facility, used for detailed molecular level
structural characterization of new organic or inorganic compounds, will
be available fo graduate student use.
24 Graduate Study in Chemistry at The Johns Hopkins University

Instrumentation
The department has significantly upgraded its mass spectrometric
instrumentation with the acquisition of the following
systems: (1) A Kratos laser desorption time-of-flight (MALDI-TOF) mass
spectrometer with linear and reflectron modes, (2) A Shimadzu gas
chromatograph mass spectrometer with both electron-impact and electron
ionization, and (3) A Thermoquest/Finnegan electrospray ionization mass
spectrometer (ESI-MS), fitted with a liquid chromatograph and with the
capability for multiple mass spectral analyses. These instruments
compliment our VG 70S high-resolution GC-mass spectrometer, which is
capable of FAB, DCI, EI, and CI spectrometry. The department also
maintains a Bruker EMX 10 /2.7 EPR spectrometer (X band and low
temperature)
In addition to computers and workstations dispersed throughout
all the individual research groups, a dedicated computer lab is housed in
Remsen Hall, with access available to all students, staff, and faculty.
Many of the faculty research laboratories have purchased or
constructed highly specialized instrumentation tailored to their specific
research objectives. These include the following: several molecular beam
apparatus, negative ion photoelectron spectrometers, ultra-high vacuum
surface analysis chambers with Auger electron and X-ray photoelectron
spectrometers, an atomic-force microscope, a time-resolved infrared
spectrometer, numerous laser systems (Nd:YAG, excimer, dye, optical
parametric oscillator, argon ion), a phase fluorimeter, a fluorescence
microscope, and nanophase material generators.
Graduate Study in
Chemistry at The Johns Hopkins University
25

Useful Information
Student Activities
As Johns Hopkins University’s main campus, the
Homewood Campus provides students with an
environment that successfully balances academics and
extracurricular activities. A strong Student Activities Office
oversees and advises over 160 student groups representing
students involved in cultural, religious, recreation, sports,
government, and special interests. Homewood is home to the JHU
Graduate Representative Organization (GRO). This graduate
student group won the 2001 National Association of Graduate-
Professional Students (NAGPS) award for Outstanding National
Graduate Student Organization.
In addition to the various student organizations, the
campus hosts other notable events, such as symposia featuring
well-known speakers, various cultural and sporting activities, and
the annual Johns Hopkins Spring Fair. This popular attraction is the
largest student run fair in the country with 150,000 visitors over the
course of three days.
Two new enhancements to campus life are the new Mattin Center for Student
Arts and Activities, and a state-of-the-art Athletic Recreation Center. The Mattin
Center offers a substantial home for student groups and organizations, while
providing a direct connection to the area’s cultural arts, such as the Baltimore
Museum of Art, which is located adjacent to the center. The new Athletic Recreation
Center is a 63,000 square foot facility housing a fully equipped gymnasium for
students, faculty and staff.
After Graduation
Many of our students do postdoctoral work, and have won prestigious postdoctoral
fellowships from the Sloan Foundation, American Cancer Society, NIH, and the
National Research Council. In the last few years they have gone on to Universities
such as Yale, Stanford, MIT, Berkeley, Caltech, the University of Chicago, and
Harvard, national laboratories such as the NIH, NIST, the Air Force Hanscom
Laboratory, and Brookhaven, or research laboratories at companies such as DuPont,
Merck, and SmithKline Beecham. Some go abroad for further study; former students
are currently in England, Japan, and Switzerland.
Alumni of the department are scattered across the country and around the
world in academic, government, and industrial positions. In the last few years, our
graduates have taken faculty positions at the University of Illinois, University of
California at Riverside, Ohio State University, Harvard University, Bryn Mawr
College, Hood College, and many other colleges and universities. Recent graduates
are now working for a number of pharmaceutical and chemical companies (Upjohn,
Pfizer, Hoechst-Roussel, Glaxo, Bristol-Meyers Squibb, Dow, Allied, 3M, Enichem
Americas, Hoechst-Celanese, to name a few). As a regular part of our colloquium
schedule, we invite former students back to describe their work and meet with
graduate students.
Housing
Near the university there is a wide selection of living quarters. Many graduate
students, single and married, take advantage of the affordable apartment buildings
adjacent to the Homewood campus. Most of the apartments in the immediate
vicinity are within easy walking distance (< 0.5 miles) of the chemistry buildings.
Additional single rooms and apartments are generally available in areas readily
accessible by car or bus. The University maintains a housing office to help students
find suitable accommodations (Housing Office, 3339 North Charles Street, Baltimore,
MD 21218, 410-516-7960). The Chemistry department also has an informal system in
place to aide students in finding suitable housing.
26 Graduate Study in Chemistry at The Johns Hopkins University

Useful Information
The Johns Hopkins University
FACULTY
E-MAIL
Zanvyl Krieger School of Arts & Sciences 410-516-8212
Graduate Admissions Office - 410-516-8174
Office of Financial Aid - 410-516-8724
Kit H. Bowen
Paul J. Dagdigian
David E. Draper
kitbowen@jhu.edu
pjdagdigian@jhu.edu
draper@jhu.edu
Office of the Registrar - Graduate Information -
410-516-8081
D. Howard Fairbrother howardf@jhu.edu
David P. Goldberg
dpg@jhu.edu
Department of Chemistry
Telephone - 410-516-7429
Fax - 410-516-8420
E-Mail - chem.grad.adm@jhu.edu
Web Site - http://www.jhu.edu/~chem
Research Professor
JOHN P. DOERING
Experimental Chemical Physics
Emeritus Faculty
DWAINE O. COWAN
Organic and Physical Chemistry
ALSOPH H. CORWIN
Biological Organic Chemistry
Marc Greenberg
Tamara L Hendrickson
Kenneth D. Karlin
Thomas Lectka
Gerald J. Meyer
Douglas Poland
Gary H. Posner
Harris J. Silverstone
Joel R. Tolman
John P. Toscano
Craig A. Townsend
David R. Yarkony
mgreenberg@jhu.edu
hendrick@jhu.edu
karlin@jhu.edu
lectka@jhu.edu
meyer@jhu.edu
poland@jhu.edu
ghp@jhu.edu
hjsilverstone@jhu.edu
jtolman@jhu.edu
jtoscano@jhu.edu
townsend@jhu.edu
yarkony@jhu.edu
JOHN W. GRYDER
Inorganic and Physical Chemistry
WALTER S. KOSKI
Physical Chemistry
BROWN L. MURR
Organic Chemistry
ALEX NICKON
Physical-Organic and Stereochemistry
DEAN W. ROBINSON
Physical Chemistry
Joint Appointments
JEREMY BERG
Biophysics, School of Medicine
BLAKE HILL
Biology, Kreiger School of Arts and Sciences
ALBERT MILDVAN
Biological Chemistry, School of Medicine
LAWRENCE PRINCIPE
History of Science Medicine and Technology/Chemistry,
Kreiger School of Arts and Sciences
MICHAEL YU
Material Science and Engineering,
Whiting School of Engineering
Graduate Study in
Chemistry at The Johns Hopkins University
27

Baltimore Map & Directions to Campus
Directions to Homewood Campus
3400 North Charles Street
Baltimore, Maryland 21218
From I-95 (southbound) or from I-695 (the Baltimore Beltway):
Take the beltway toward Towson to exit 25. Take Charles
Street south for about 7 miles (when Charles Street splits
a block after Loyola College and Cold Spring Lane, take
the right fork). As you approach the university and cross
University Parkway, continue southbound but be sure to
jog right onto the service road. After you pass the university
on the right, turn right onto Art Museum Drive. Just
after the Baltimore Museum of Art, bear right at the traffic
island onto Wyman Park Drive. Take an almost immediate
right through the university gates. A visitors' lot
and parking meters will be on the left.
From I-95 (northbound):
Take exit 53 onto I-395 north toward downtown
Baltimore, then take the exit to Martin Luther King Jr.
Boulevard and follow the directions from Martin Luther
King Junior Boulevard below.
From Maryland 295 (the Baltimore-Washington Parkway):
Entering Baltimore, the parkway becomes Russell Street.
Stay on Russell Street until (with the new Baltimore
Ravens stadium to your right and Oriole Park at Camden
Yards looming before you) you reach the right-hand exit
marked Martin Luther King Jr. Boulevard (look carefully
for this; the signs are small). This exit will put you very
briefly on a service road parallel to Russell Street. Stay to
the left and take the ramp marked Martin Luther King Jr.
Boulevard. Follow the directions (below) from Martin
Luther King Jr. Boulevard.
From Martin Luther King Jr. Boulevard:
Take King Boulevard north until it ends at Howard Street
(remain in one of the middle lanes of King Boulevard to
avoid a premature forced right or left turn). Turn left at
Howard Street and proceed about 2 miles. One block
past 29th Street, turn left at the traffic island (just before
the Baltimore Museum of Art) onto Wyman Park Drive.
Take an almost immediate right through the university
gates. A visitors' lot and parking meters will be on the
left.
From the Jones Falls Expressway (I-83) southbound:
Take the 28th Street exit and go left on 28th Street. Turn
left on North Howard Street. One block past 29th Street,
turn left at the traffic island (just before the Baltimore
Museum of Art) onto Wyman Park Drive. Take an almost
immediate right through the university gates. A visitors'
lot and parking meters will be on the left.
From Baltimore's Penn Station:
From Penn Station, you can catch the Hopkins shuttle
bus which will take you to the Homewood, Peabody, or
medical campuses. There is no charge to take the shuttle.
If you opt to take a taxi, the fee should be quite modest.
The university is very close to the train station.
28 Graduate Study in Chemistry at The Johns Hopkins University