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Current Physical Chemistry

Editor-in-Chief

ISSN (Print): 1877-9468
ISSN (Online): 1877-9476

The Protein Folding Mechanism Revealed by the Folding Free Energy Landscape Analysis and Denaturation Simulations

Author(s): Qiang Shao and Yi Qin Gao

Volume 2, Issue 1, 2012

Page: [33 - 44] Pages: 12

DOI: 10.2174/1877946811202010033

Price: $65

Abstract

α-helix and β-hairpin are the two principal secondary structures in proteins. A large number of experimental and theoretical kinetics and thermodynamics studies of the folding and unfolding of α-helix and β-hairpin structured polypeptides and proteins have been performed. Different theoretical models have been proposed to explain their folding mechanisms. Inconsistencies exist among the various models, which essentially reflect the different understanding of how individual structural elements affect the folding process and stability of protein structures. The present review mainly summarizes our recent simulation studies of the structure stability, folding and unfolding (denaturation) mechanism of various α-helix bundle and β-structure systems.

Keywords: Protein folding, Free energy landscape analysis, Molecular dynamics simulation, α-helix bundle, hydrophobic, Urea Denaturation, Helix, mutation, replica


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