Journal article
Hydrogen bonding increases packing density in the protein interior
Proteins, structure, function, and bioinformatics, Vol.63(2), pp.278-282
05/01/2006
DOI: 10.1002/prot.20826
PMID: 16353166
Abstract
The contribution of hydrogen bonds and the burial of polar groups to protein stability is a controversial subject. Theoretical studies suggest that burying polar groups in the protein interior makes an unfavorable contribution to the stability, but experimental studies show that burying polar groups, especially those that are hydrogen bonded, contributes favorably to protein stability. Understanding the factors that are not properly accounted for by the theoretical models would improve the models so that they more accurately describe experimental results. It has been suggested that hydrogen bonds may contribute to protein stability, in part, by increasing packing density in the protein interior, and thereby increasing the contribution of van der Waals interactions to protein stability. To investigate the influence of hydrogen bonds on packing density, we analyzed 687 crystal structures and determined the volume of buried polar groups as a function of their extent of hydrogen bonding. Our findings show that peptide groups and polar side chains that form hydrogen bonds occupy a smaller volume than the same groups when they do not form hydrogen bonds. For example, peptide groups in which both polar groups are hydrogen bonded occupy a volume, on average, 5.2 Å3 less than a peptide group that is not hydrogen bonded. © 2005 Wiley-Liss, Inc.
Details
- Title: Subtitle
- Hydrogen bonding increases packing density in the protein interior
- Creators
- David Schell - Texas A&M UniversityJerry Tsai - Texas A&M UniversityJ. Martin Scholtz - Texas A&M UniversityC. Nick Pace - Texas A&M University System
- Resource Type
- Journal article
- Publication Details
- Proteins, structure, function, and bioinformatics, Vol.63(2), pp.278-282
- Publisher
- Wiley Subscription Services, Inc., A Wiley Company
- DOI
- 10.1002/prot.20826
- PMID
- 16353166
- ISSN
- 0887-3585
- eISSN
- 1097-0134
- Number of pages
- 5
- Language
- English
- Date published
- 05/01/2006
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293080902771
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