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2014 ; 588
(14
): 2177-84
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Forces stabilizing proteins
#MMPMID24846139
Nick Pace C
; Scholtz JM
; Grimsley GR
FEBS Lett
2014[Jun]; 588
(14
): 2177-84
PMID24846139
show ga
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±0.5 kcal/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±0.8 kcal/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.
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