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PDBsum entry 4b2c
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Hydrolase/hydrolase inhibitor
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PDB id
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4b2c
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References listed in PDB file
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Key reference
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Title
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Thermodynamic signatures in macromolecular interactions involving conformational flexibility.
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Authors
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A.Menzel,
P.Neumann,
C.Schwieger,
M.T.Stubbs.
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Ref.
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Biol Chem, 2014,
395,
905-911.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Abstract The energetics of macromolecular interactions are complex, particularly
where protein flexibility is involved. Exploiting serendipitous differences in
the plasticity of a series of closely related trypsin variants, we analyzed the
enthalpic and entropic contributions accompanying interaction with L45K-eglin C.
Binding of the four variants show significant differences in released heat,
although the affinities vary little, in accordance with the principle of
enthalpy-entropy compensation. Binding of the most disordered variant is almost
entirely enthalpically driven, with practically no entropy change. As structures
of the complexes reveal negligible differences in protein-inhibitor contacts, we
conclude that solvent effects contribute significantly to binding affinities.
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