Please use this identifier to cite or link to this item: https://doi.org/10.1002/1097-0282(200103)58:33.0.CO;2-9
Title: Hydrogen-bond disruption probability in proteins by a modified self-consistent harmonic approach
Authors: Cao, Z.W. 
Chen, Y.Z. 
Keywords: Hydrogen-bond
Protein dynamics
Protein folding
Protein stability
Thermal fluctuational hydrogen bond disruption
Vibrational normal modes
Issue Date: 2001
Citation: Cao, Z.W.,Chen, Y.Z. (2001). Hydrogen-bond disruption probability in proteins by a modified self-consistent harmonic approach. Biopolymers 58 (3) : 319-328. ScholarBank@NUS Repository. https://doi.org/10.1002/1097-0282(200103)58:33.0.CO;2-9
Abstract: Modified self-consistent harmonic approach was employed to calculate the probability for the disruption of each individual hydrogen bonds (H bonds) in x-ray crystal structure of several proteins. The computed probability for 82% of intraprotein and water-protein H bonds studied were found to be roughly consistent with estimated free energies from protein engineering and hydrogen exchange experiments. Hydrogen bonds have been proposed as part of a stereochemical code for protein folding. Proteins fold into unique three-dimensional structures; therefore those bonds involved in the folding code are expected to be stable. We have applied this method to tens of hydrogen bonds in a protein assumed to be involved in the folding code of a protein. 58% of these H bonds were found to have a lower disruption probability (- 1.8 kcal/mol). Our results showed that modified self-consistent harmonic approach might be explored as a method supplement to existing methods in analysis of hydrogen bonds in proteins. © 2001 John Wiley & Sons, Inc.
Source Title: Biopolymers
URI: http://scholarbank.nus.edu.sg/handle/10635/104796
ISSN: 00063525
DOI: 10.1002/1097-0282(200103)58:33.0.CO;2-9
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Page view(s)

29
checked on Jul 20, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.