"Exploring the Interplay between Topology and Secondary Structural Form" by Margaret S. Cheung, John M. Finke et al.
 

Exploring the Interplay between Topology and Secondary Structural Formation in the Protein Folding Problem

Publication Date

10-1-2003

Document Type

Article

Abstract

Simple models with a single bead representation (Cα models) have been successful in providing a qualitative understanding of the folding mechanism of small globular proteins. Can we go beyond this qualitative understanding and make more detailed quantitative connections to experiments? To achieve this goal, a tractable framework of protein representations whose complexity falls between Cα and all-atom representations is needed to address different energetic competing factors during folding events. Such a model conserves the low computational expense inherent in minimalist models while enhancing the understanding of side-chain packing not existent in simple Cα models. In this work, we present a minimalist representation of protein structures that are used to investigate the competition between native side-chain contacts and nonspecific backbone hydrogen bonds. Our results suggest that native tertiary contacts and dihedrals force the nonspecific hydrogen bonds to adopt native configurations and retain a funneled landscape. In addition, the use of an angular component in the hydrogen bond interaction prevents non-native conformations.

Publication Title

The Journal of Physical Chemistry B

Volume

107

Issue

40

First Page

11193

Last Page

11200

DOI

10.1021/jp034441r

Publisher Policy

pre-print, post-print

This document is currently not available here.

Find in your library

Share

COinS