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Entropy in biological binding processes: Estimation of translational entropy loss

Murphy, Kenneth P., Xie, Dong, Thompson, Kelly S., Amzel, L. Mario, Freire, Ernesto·1994·Proteins: Structure, Function, and Bioinformatics

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.

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Metadata

Authors
Murphy, K. P., Xie, D., Thompson, K. S., Amzel, L. M., & Freire, E.
Venue
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Published
1994-01
Volume
18
Issue
1
Pages
63-67
ISSN
  • 0887-3585 (ISSN-L)
  • 1097-0134
OpenAlex
W2005367001
Cited by
178
References
0
FWCI
10.08
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Entropy in biological binding processes: Estimation of translational entropy loss. https://app.cochat.ai/papers/10.1002/prot.340180108
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Murphy, K. P., Xie, D., Thompson, K. S., Amzel, L. M., & Freire, E. (1994). Entropy in biological binding processes: Estimation of translational entropy loss. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340180108

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.