Entropy in biological binding processes: Estimation of translational entropy loss

Kenneth P. Murphy; Dong Xie; Kelly S. Thompson; L. Mario Amzel; Ernesto Freire

doi:10.1002/prot.340180108

Entropy in biological binding processes: Estimation of translational entropy loss

Kenneth P. Murphy, Dong Xie, Kelly S. Thompson, L. Mario Amzel, Ernesto Freire

Research output: Contribution to journal › Article › peer-review

156 Scopus citations

Abstract

The loss of translational degrees of freedom makes an important, unfavorable contribution to the free energy of binding. Examination of experimental values suggest that calculation of this entropy using the Sackur–Tetrode equation produces largely overestimated values. Better agreement is obtained using the cratic entropy. Theoretical considerations suggest that the volumes available for the movement of a ligand in solution and in a complex are rather similar, suggesting also that the cratic entropy provides the best estimate of the loss of translational entropy. © 1994 John Wiley & Sons, Inc.

Original language	English (US)
Pages (from-to)	63-67
Number of pages	5
Journal	Proteins: Structure, Function, and Bioinformatics
Volume	18
Issue number	1
DOIs	https://doi.org/10.1002/prot.340180108
State	Published - Jan 1994

Keywords

binding energetics
entropy
macromolecular interactions
thermodynamics
translational entropy

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.340180108

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abstract = "The loss of translational degrees of freedom makes an important, unfavorable contribution to the free energy of binding. Examination of experimental values suggest that calculation of this entropy using the Sackur–Tetrode equation produces largely overestimated values. Better agreement is obtained using the cratic entropy. Theoretical considerations suggest that the volumes available for the movement of a ligand in solution and in a complex are rather similar, suggesting also that the cratic entropy provides the best estimate of the loss of translational entropy. {\textcopyright} 1994 John Wiley & Sons, Inc.",

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author = "Murphy, {Kenneth P.} and Dong Xie and Thompson, {Kelly S.} and Amzel, {L. Mario} and Ernesto Freire",

year = "1994",

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AB - The loss of translational degrees of freedom makes an important, unfavorable contribution to the free energy of binding. Examination of experimental values suggest that calculation of this entropy using the Sackur–Tetrode equation produces largely overestimated values. Better agreement is obtained using the cratic entropy. Theoretical considerations suggest that the volumes available for the movement of a ligand in solution and in a complex are rather similar, suggesting also that the cratic entropy provides the best estimate of the loss of translational entropy. © 1994 John Wiley & Sons, Inc.

KW - binding energetics

KW - entropy

KW - macromolecular interactions

KW - thermodynamics

KW - translational entropy

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Entropy in biological binding processes: Estimation of translational entropy loss

Abstract

Keywords

ASJC Scopus subject areas

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