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
DC Field | Value | |
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dc.title | Hydrogen-bond disruption probability in proteins by a modified self-consistent harmonic approach | |
dc.contributor.author | Cao, Z.W. | |
dc.contributor.author | Chen, Y.Z. | |
dc.date.accessioned | 2014-10-28T03:11:53Z | |
dc.date.available | 2014-10-28T03:11:53Z | |
dc.date.issued | 2001 | |
dc.identifier.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 | |
dc.identifier.issn | 00063525 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/104796 | |
dc.description.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. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/1097-0282(200103)58:33.0.CO;2-9 | |
dc.source | Scopus | |
dc.subject | Hydrogen-bond | |
dc.subject | Protein dynamics | |
dc.subject | Protein folding | |
dc.subject | Protein stability | |
dc.subject | Thermal fluctuational hydrogen bond disruption | |
dc.subject | Vibrational normal modes | |
dc.type | Article | |
dc.contributor.department | COMPUTATIONAL SCIENCE | |
dc.description.doi | 10.1002/1097-0282(200103)58:33.0.CO;2-9 | |
dc.description.sourcetitle | Biopolymers | |
dc.description.volume | 58 | |
dc.description.issue | 3 | |
dc.description.page | 319-328 | |
dc.description.coden | BIPMA | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Staff Publications |
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