Dresden 2003 – wissenschaftliches Programm

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CPP: Chemische Physik und Polymerphysik

CPP 6: Computational Soft Matter Physics

CPP 6.2: Hauptvortrag

Dienstag, 25. März 2003, 10:00–10:30, ZEU/160

Protein Hydration, Ligand Binding and the Glass Transition — •Jeremy C. Smith — The BioComputing Group, IWR, Universität Heidelberg, 69120 Heidelber

Solvent plays an important role in modulating internal motions of proteins. It influences the dynamics by interacting with protein directly and screens the charge-charge interaction within the protein molecule and also between the protein and its ligands. The effects of the solvent have been investigated by computer simulations which were compared with experimental measurements. Experimental and computer simulation studies have revealed the presence of a glasslike transition in the internal dynamics of hydrated proteins at around 200 K involving an increase of the amplitude of anharmonic dynamics. This increase in flexibility has been correlated with the onset of protein activity and ligand binding. The results of our computer simulations show that the protein transition is driven by a dynamical transition in the hydration water that induces anharmonic fluctuations primarily in side-chains in the external regions of the protein.