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Effect of rotation on the diffusion-controlled rate of ligand-protein association.
Open accessAbstract
The rate of binding a fairly large ligand molecule to a protein is reduced below the usual diffusion-controlled rate by the requirement of a certain rotational orientation. A simple, approximate treatment of this effect is given for special cases of spherical and ellipsoidal ligands. As the center of an ellipsoidal ligand approaches a protein surface, there is an effective repulsive potential between ligand and surface owning to restricted rotation of the ligand. The frequency factor kT/h of the Eyring rate theory is replaced in these reactions involving diffusion in solution by D/Rlambda, where D = diffusion coefficient of ligand, lambda = thermal deBroglie wavelength of ligand, and R = "capture" distance around the binding site on the protein.
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Cited by
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Chan, H. S., & Dill, K. A. (1998) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19980101)30:1<2::aid-prot2>3.0.co;2-r · Cited by 438
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Shoup, D., & Szabo, A. (1982) · Biophysical Journal · doi:10.1016/s0006-3495(82)84455-x · Cited by 428
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Dayton, M. A., Brown, J. C., Stutts, K. J., & Wightman, R. M. (1980) · Analytical Chemistry · doi:10.1021/ac50056a040 · Cited by 330
Metadata
- Authors
- Hill, T. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1975-12
- Volume
- 72
- Issue
- 12
- Pages
- 4918-4922
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2038220682
- Cited by
- 166
- References
- 0
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- green
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