XIII European Conference on the Spectroscopy of ... - ecsbm 2009

Palermo, August 28 – September 2, 2009 13 th ECSBM −−−− Book of Abstracts
Protein dynamics and functionality: the role of
hydration shell waters
JOEL M. FRIEDMAN
Dept of Physiology and Biophysics, Albert Einstein College of Medicine,
Bronx, New York USA 10461
It has become fully apparent that protein functionality requires that the protein be dynamically
active and that solvent motions are needed for activation of functionally important protein
dynamics. In attempting to study the interplay between dynamics and functionality one is
confronted with the complication that there is myriad of different types of dynamics displayed by
proteins. How to organize these dynamics into a meaningful and workable scheme is a challenge.
One promising approach is based on Frauenfelder and coworkers solvent slaving concept which
defines a hierarchy of protein dynamics based on which category of solvent motion controls the
enthalpic barrier associated with specific conformational fluctuations and relaxations. This concept
dictates that an overall approach to the study of the dynamical basis for protein functionality
include four elements: function, protein dynamics, solvent motions and their interdependence. The
presentation will describe how we have used sol-gel and glass matrices in combination with an
extension of the solvent slaving concept in the form our proposed Protein Dynamic State Model to
link functionality, conformational dynamics and solvent properties. Additionally we will present
advances in the use of several spectroscopic tools including vibronic side band spectroscopy to
probe the response of hydration shell waters to added osmolytes and the correlated impact on
protein properties. A general picture based on these studies will be presented that links hydration
shell water properties, dynamics and functionality.
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