Protein folding mediated by solvation: water expelling and formation of the hydrophobic core occurs after the structure collapse

Preprint

31 March 2002

preprint
Published by arXiv in arXiv

https://doi.org/10.48550/arXiv.cond-mat/0204014

Abstract

The interplay between structure-search of the native structure and desolvation in protein folding has been explored using a minimalist model. These results support a folding mechanism where most of the structural formation of the protein is achieved before water is expelled from the hydrophobic core. This view integrates water expulsion effects into the funnel energy landscape theory of protein folding. Comparisons to experimental results are shown for the SH3 protein. After the folding transition, a near-native intermediate with partially solvated hydrophobic core is found. This transition is followed by a final step that cooperatively squeezes out water molecules from the partially hydrated protein core.

Keywords

All Related Versions

Version 1, 2002-03-31, ArXiv
Published version: Proceedings of the National Academy of Sciences, 99 (2), 685.

This publication has 0 references indexed in Scilit: