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|Title:||Hydrogen-bond disruption probability in proteins by a modified self-consistent harmonic approach||Authors:||Cao, Z.W.
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|
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