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PDBsum entry 4j5k
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References listed in PDB file
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Key reference
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Title
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Contribution of hydrogen bonds to protein stability.
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Authors
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C.N.Pace,
H.Fu,
K.Lee fryar,
J.Landua,
S.R.Trevino,
D.Schell,
R.L.Thurlkill,
S.Imura,
J.M.Scholtz,
K.Gajiwala,
J.Sevcik,
L.Urbanikova,
J.K.Myers,
K.Takano,
E.J.Hebert,
B.A.Shirley,
G.R.Grimsley.
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Ref.
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Protein Sci, 2014,
23,
652-661.
[DOI no: ]
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PubMed id
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Abstract
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Our goal was to gain a better understanding of the contribution of the burial of
polar groups and their hydrogen bonds to the conformational stability of
proteins. We measured the change in stability, Δ(ΔG), for a series of hydrogen
bonding mutants in four proteins: villin headpiece subdomain (VHP) containing 36
residues, a surface protein from Borrelia burgdorferi (VlsE) containing 341
residues, and two proteins previously studied in our laboratory, ribonucleases
Sa (RNase Sa) and T1 (RNase T1). Crystal structures were determined for three of
the hydrogen bonding mutants of RNase Sa: S24A, Y51F, and T95A. The structures
are very similar to wild type RNase Sa and the hydrogen bonding partners form
intermolecular hydrogen bonds to water in all three mutants. We compare our
results with previous studies of similar mutants in other proteins and reach the
following conclusions. (1) Hydrogen bonds contribute favorably to protein
stability. (2) The contribution of hydrogen bonds to protein stability is
strongly context dependent. (3) Hydrogen bonds by side chains and peptide groups
make similar contributions to protein stability. (4) Polar group burial can make
a favorable contribution to protein stability even if the polar groups are not
hydrogen bonded. (5) The contribution of hydrogen bonds to protein stability is
similar for VHP, a small protein, and VlsE, a large protein.
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