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Article: Forces stabilizing proteins

Nick Pace, C / J. Martin Scholtz / Gerald R. Grimsley

Federation of European Biochemical Societies FEBS letters. 2014 June 27, v. 588, no. 14

2014  

Abstract: The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site-directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydrophobic ...

Abstract The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site-directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydrophobic and hydrogen bonding variants. (1) Based on studies of 138 hydrophobic interaction variants in 11 proteins, burying a –CH2− group on folding contributes 1.1±0.5kcal/mol to protein stability. (2) The burial of non-polar side chains contributes to protein stability in two ways: first, a term that depends on the removal of the side chains from water and, more importantly, the enhanced London dispersion forces that result from the tight packing in the protein interior. (3) Based on studies of 151 hydrogen bonding variants in 15 proteins, forming a hydrogen bond on folding contributes 1.1±0.8kcal/mol to protein stability. (4) The contribution of hydrogen bonds to protein stability is strongly context dependent. (5) Hydrogen bonds by side chains and peptide groups make similar contributions to protein stability. (6) Polar group burial can make a favorable contribution to protein stability even if the polar group is not hydrogen bonded. (7) Hydrophobic interactions and hydrogen bonds both make large contributions to protein stability.
Keywords hydrogen bonding ; hydrophobic bonding ; hydrophobicity ; proteins ; site-directed mutagenesis
Language English
Dates of publication 2014-0627
Size p. 2177-2184.
Publishing place Elsevier B.V.
Document type Article
ZDB-ID 212746-5
ISSN 1873-3468 ; 0014-5793
ISSN (online) 1873-3468
ISSN 0014-5793
DOI 10.1016/j.febslet.2014.05.006
Shelf mark
Z 2005/702: Show issues
Z 5.4: Show issues
Database NAL-Catalogue (AGRICOLA)

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