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PDBsum entry 2rq8
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References listed in PDB file
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Key reference
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Title
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Structural basis for unfolding pathway-Dependent stability of proteins: vectorial unfolding versus global unfolding.
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Authors
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K.Yagawa,
K.Yamano,
T.Oguro,
M.Maeda,
T.Sato,
T.Momose,
S.Kawano,
T.Endo.
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Ref.
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Protein Sci, 2010,
19,
693-702.
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PubMed id
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Abstract
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Point mutations in proteins can have different effects on protein stability
depending on the mechanism of unfolding. In the most interesting case of I27,
the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields
opposite effects on protein stability during denaturant-induced "global
unfolding" versus "vectorial unfolding" by mechanical pulling force or cellular
unfolding systems. Here, we assessed the reason for the different effects of the
Y9P mutation of I27 on the overall molecular stability and N-terminal unraveling
by NMR. We found that the Y9P mutation causes a conformational change that is
transmitted through beta-sheet structures to reach the central hydrophobic core
in the interior and alters its accessibility to bulk solvent, which leads to
destabilization of the hydrophobic core. On the other hand, the Y9P mutation
causes a bend in the backbone structure, which leads to the formation of a more
stable N-terminal structure probably through enhanced hydrophobic interactions.
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