Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
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Symposium Life Sciences on the Nanometer Scale - Physics Meets Biology Mittwoch<br />
optical properties of the whole complex.<br />
SYLS 3.22 Mi 16:00 B<br />
Ab-initio vibrational analysis of the secondary structure of proteins<br />
— •Lars Ismer 1 , Joel Ireta 1 und Jörg Neugebauer 2 —<br />
1 FHI Berlin — 2 Universität Paderborn<br />
For a detailed understanding of protein functionality an accurate description<br />
of their dynamical properties is crucial. However, so far ab-initio<br />
based studies on realistic structures going beyond the primary structure<br />
are rare, particularly with respect to vibrational properties. We have therefore<br />
performed a full ab-initio DFT-PBE based harmonic vibrational<br />
analysis of infinite poly-alanine and -glycine chains in two different secondary<br />
conformations: the infinite α-helical conformation, as model for the<br />
most ubiquitous native secondary conformation stabilized by hydrogen<br />
bonds (hb) and the fully extended conformation (FES), as a reference<br />
system where hb’s are absent. By comparing the phonon dispersion relation<br />
of α-helix and FES we were able to extract a direct ”fingerprint”<br />
of the hb’s and their cooperativity in specific high frequent vibrational<br />
branches. We also observed that constraining the peptide chain to the<br />
helical conformation leads to significant blue-shifts in the low frequent<br />
backbone vibrations. A thermodynamic analysis based on these results<br />
revealed that the vibrational contributions of the free energy significantly<br />
lower the stability of the α-helix with respect to the FES by about 0.8<br />
kcal/mol at 300K.<br />
SYLS 3.23 Mi 16:00 B<br />
Optical characterisation of artifical confinements for protein<br />
folding — •Johannes Hohlbein 1 , Ulrike Rehn 1 , and Ralf B.<br />
Wehrspohn 2 — 1 Max-Planck-Institute of Microstructure Physics,<br />
Weinberg 2, 06120 Halle, Germany — 2 Department of Physics,<br />
University of Paderborn, Warburger Str. 100, 33098 Paderborn,<br />
Germany<br />
We present a new method to characterize in-situ the optical thickness<br />
of porous alumina films by the use of photoluminescence-induced Fabry-<br />
Pèrot-interferences. Additionally we show, that the use of different electrolytes<br />
yields different photoluminescence pattern. A second experiment<br />
allows to determine the degree of filling of the pores by a liquid which is<br />
of importance when using the pores as templates for protein folding. First<br />
studies of the influence of geometrical confinement on protein folding will<br />
be presented.<br />
Porous oxide growth on aluminium under anodic bias in various electrolytes<br />
has been studied for nearly 50 years. Recently, porous anodic<br />
alumina (PAA) films have been used to prepare nanostructures for a<br />
wide range of applications. In order to use porous alumina as template<br />
for protein folding in-situ optical measurements of their thickness as well<br />
as the degree of filling are required. It has been shown, that porous alumina<br />
exhibits a photoluminescence (PL) signal. We will use the PL pattern<br />
to determine the thickness and the degree of filling by Fabry-Pèrotinterferences.<br />
SYLS 3.24 Mi 16:00 B<br />
Neuronale Synchronität in biologisch plausiblen exzitatorischen<br />
Netzwerken: Entstehung und Modulation — •K. Kube 1 , V.<br />
Spravedlyvyy 1 , A. Herzog 1 , B. Michaelis 1 , A. de Lima 2 , T.<br />
Opitz 2 , T. Voigt 2 , A. Reiher 3 , A. Krtschil 3 , S. Günther 3 , H.<br />
Witte 3 und A. Krost 3 — 1 Institut für Elektronik, Signalverarbeitung<br />
und Kommunikationstechnik, Otto-von-Guericke-Universität Magdeburg<br />
— 2 Institut für Physiologie, Otto-von-Guericke-Universität Magdeburg<br />
— 3 Institut für Experimentelle Physik, Otto-von-Guericke-Universität<br />
Magdeburg<br />
Detaillierte Kompartimentmodelle von Einzelneuronen sind oft benutzt<br />
worden, um das Gehirn als modulare elektrische Apparatur darzustellen.<br />
Wir präsentieren eine biologisch realistische Simulation von<br />
Netzwerk-Eigendynamik, wie sie in Zellkulturen des frühen zerebralen<br />
Kortex von Wirbeltieren abläuft. Dabei wird die Entwicklung der<br />
natürlichen Vernetzungstruktur nachgebildet, in der verschiedene funktionelle<br />
Neuronentypen interagieren. Ausgehend von spontaner elektrischer<br />
Aktivität einzelner Neurone werden in massiven Simulationen Eigenarten<br />
der elektrischen Dynamik des Netzwerks und deren gezielte<br />
Beeinflussung gezeigt sowie mit der in-vitro-gemessenen Aktivität verglichen,<br />
die in Verbindung mit zellulären Lernmechanismen (Hebb-LTP)<br />
wechselwirken können, um sich an Muster äußerer Reize anzupassen. Abschließend<br />
wird diskutiert, auf welche Art man in spontan feuernden Zellen,<br />
die über zufällige, rekurrente Strukturen von Netzwerken verbunden<br />
werden, von Organisation sprechen kann.<br />
SYLS 3.25 Mi 16:00 B<br />
Protein adsorption on tailored substrates — •Hubert Mantz,<br />
Anthony W. Quinn, and Karin Jacobs — Experimental Physics,<br />
Saarland University, POB 151 150, 66041 Saarbrücken<br />
It has long been established that bacterial plaque plays an essential role<br />
in the development of oral diseases such as dental caries. Dental plaque<br />
consists of a diversity of different components, which makes it difficult to<br />
determine the mechanism for their formation and growth. Understanding<br />
them would enhance the field of preventative dentistry enabling restorative<br />
materials to be tailored to resist bacterial attachment or have some<br />
antibacterial effect.<br />
We try to get an insight in these mechanisms by using ellipsometry, a<br />
non-destructive optical method for determining film thickness and optical<br />
properties of the sample to be studied. These experiments can measure<br />
the adsorption kinetics of purified salivary proteins on tailored substrates.<br />
By using AFM and wettability analysis, the composition of the surfaces<br />
can be controlled and described.<br />
SYLS 3.26 Mi 16:00 B<br />
Picosecond dynamics of bacterial porins investigated by<br />
quasi-elastic neutron scattering — •Marie Plazanet 1 , Cecile<br />
Bon 2 , Franck Gabel 3 , Sylviane Julien 2 , Peter Timmins 1 ,<br />
and Guiseppe Zaccai 3 — 1 Institut Laue Langevin, 6 rue Jules<br />
Horowitz, 38042 Grenoble Cedex 9, France — 2 CNRS/IPBS, 205 route<br />
de Narbonnes, 31077 Toulouse cedex, France — 3 IBS, 41, rue Jules<br />
Horowitz, 38027 Grenoble Cedex 1, France<br />
The survival of bacteria requires a continuous exchange of molecules<br />
across the cell wall. Porins, a large class of membrane proteins, are involved<br />
in the transport of small hydrophilic molecules across the outer<br />
membrane. Porins have peculiar structural features; they fold in a multistranded,<br />
closed beta-sheet, exposed to the hydrophobic membrane core<br />
on one side and an aqueous channel on the other. Dynamics of these extremely<br />
stable proteins clearly modulate the pore activity (i.e. biological<br />
activity of the porin), and there is good evidence that this dynamics is<br />
modulated by the dynamics of the lipids surrounding the porins.<br />
Experiments have been undertaken on outer membrane fractions of<br />
E.Coli, with the natural asymmetric lipid distribution (lipopolysaccharides<br />
in the outer leaflet and various phospholipids in the inner leaflet).<br />
Samples enriched in porins and samples depleted in porins have been investigated<br />
to probe both lipid and porin contribution. While data are still<br />
under study, preliminary results show that both systems clearly exhibit<br />
very different dynamics on the pico-second timescale. A brief comparison<br />
with corresponding results on the bacteriorhodospsin, a representative of<br />
the membrane proteins folded in an helix-bundle, will be done.<br />
SYLS 3.27 Mi 16:00 B<br />
Controlled proliferation of living cells on UV-light modified polymers<br />
— •Thomas Gumpenberger 1 , Johannes Heitz 1 , Dieter<br />
Baeuerle 1 und Christoph Romanin 2 — 1 Angewandte Physik, Universitaet<br />
Linz, Austria — 2 Biophysik, Universitaet Linz, Austria<br />
We demonstrated the controlled proliferation of human umbilical endothelial<br />
cells (HUVEC) on UV-light modified polymer samples. The polymers<br />
under investigation were either polytetrafluoroethylene (PTFE)<br />
or polyethyleneterephtalate (PET), which are among the most frequently<br />
employed biomaterials in reconstructive medicine. The PTFE surfaces<br />
were modified by exposure to the ultraviolet (UV) light of a Xe2*-excimer<br />
lamp at a wavelength of 172 nm in an ammonia atmosphere. The irradiation<br />
led to an efficient exchange of the F-atoms in the surface by other<br />
chemical moieties. In-vitro, this resulted in a significant increase in the<br />
number of adhering cells 1 day after seeding and in the formation of a<br />
confluent cell layer after 3 to 8 days. The results were comparable or even<br />
better than those obtained on standard polystyrene petri-dishes used in<br />
cell cultivation. Similar studies were performed on PET.<br />
SYLS 3.28 Mi 16:00 B<br />
Electrolytic fabrication of SNOM aperture-sensors — •Carola<br />
Haumann, Christoph Pelargus, Robert Ros, and Dario Anselmetti<br />
— Experimental Biophysics and Applied Nanosciences, Faculty<br />
of Physics, Bielefeld University, Universitaetsstrasse 25, 33615 Bielefeld,<br />
Germany<br />
The resolution achievable with scanning near-field optical microscopy<br />
(SNOM) is determined by the optical quality of the near-field sensors.<br />
We present a method to fabricate reproducibly aperture probes with diameters<br />
in the sub 100nm range by solid state electrolysis. The method,<br />
originally invented by A. Bouhelier et al., was further developed by in-