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Titolo:
Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water molecule in bovine pancreatic trypsin inhibitor
Autore:
Fischer, S; Smith, JC; Verma, CS;
Indirizzi:
Univ York, Dept Chem, Struct Biol Lab, York YO1 5DD, N Yorkshire, England Univ York York N Yorkshire England YO1 5DD YO1 5DD, N Yorkshire, England Univ Heidelberg, IWR, D-69120 Heidelberg, Germany Univ Heidelberg Heidelberg Germany D-69120 , D-69120 Heidelberg, Germany
Titolo Testata:
JOURNAL OF PHYSICAL CHEMISTRY B
fascicolo: 33, volume: 105, anno: 2001,
pagine: 8050 - 8055
SICI:
1520-6106(20010823)105:33<8050:DTVECO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
STRUCTURAL WATER; ENERGY LANDSCAPE; BOUND WATER; PROTEINS; DYNAMICS; HYDRATION; SITE; ASSOCIATION; ACTIVATION; CAVITIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Verma, CS Univ York, Dept Chem, Struct Biol Lab, York YO1 5DD, N Yorkshire, England Univ York York N Yorkshire England YO1 5DD N Yorkshire, England
Citazione:
S. Fischer et al., "Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water molecule in bovine pancreatic trypsin inhibitor", J PHYS CH B, 105(33), 2001, pp. 8050-8055

Abstract

Using normal-mode analysis, the vibrational entropy change on the burial of a crystallographically well-ordered water molecule in bovine pancreatic trypsin inhibitor (BPTI) is dissected. The vibrational entropy content of the complex is 13.4 cal mol(-1) K-1 higher than that of the unbound protein. A detailed analysis is performed of how the translational and rotational degrees of freedom of the isolated water molecule are transformed into vibrational modes in the complex. This process is shown to be well described by amodel of the complex in which the water molecule librates in a rigid protein cage. These librational modes contribute 9.4 cal mol(-1) K-1 to the entropy change. The remaining 4 cal mol(-1) K-1 arises from increased protein flexibility due to softening of the delocalized modes, mostly in the frequency range below 50 cm(-1). The dominant librational entropy effect suggests a method by which an estimation of the vibrational contribution to ligand binding can be efficiently computed.

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Documento generato il 09/12/19 alle ore 03:42:06