Regensburg 2007 – wissenschaftliches Programm
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DY: Fachverband Dynamik und Statistische Physik
DY 30: Poster II
DY 30.24: Poster
Donnerstag, 29. März 2007, 16:00–18:00, Poster D
Solvent dependence of protein secondary structures — •Hendrik Hansen-Goos1,2, Roland Roth1,2, Klaus Mecke3, and Siegfried Dietrich1,2 — 1Max-Planck-Institut für Metallforschung, Heisenbergstr. 3, 70569 Stuttgart — 2ITAP, Universität Stuttgart, Pfaffenwaldring 57, 70569 Stuttgart — 3ITP, Universität Erlangen-Nürnberg, Staudtstr. 7, 91058 Erlangen
Predicting the native state of a protein from a given sequence of amino acids is a task which has not been solved satisfactorily so far. An understanding of the mechanisms involved in protein folding is highly desirable as the 3D structure of a protein determines its function. Many approaches focus on energetic contributions from interaction between the amino acids and interaction with the solvent. There is, however, a contribution to the solvation free energy arising from the solvent entropy which varies for different protein configurations. We calculate solvent entropies for a protein represented in the simple tube model. Using the so-called morphometric approach, which makes calculations very efficient, we are able to scan over a large range of solvent configurations. For the particular case of a hard-sphere solvent, we discern regions where either a tightly packed helix, a sheetlike structure, or some unwinded helix minimizes the solvation free energy. Extensions to more realistic solvents and hydrophilic and hydrophobic interactions are presented.