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The dielectric constant of a folded protein
Abstract
The goal of this paper is to obtain a theoretical estimate of the dielectric constant of a folded protein. To this end, we develop a form of the Kirkwood–Fröhlich dielectric theory that applies to polar solids and folded proteins. The resulting theory incorporates a factor expressing the degree to which dipolar groups are constrained within the material's structure, as well as a generalized form of Kirkwood's correlation factor. The theory is applied to a hypothetical isotropic protein composed of randomly oriented α‐helices and having a number density of dipolar groups equal to that found in actual proteins. The factor of constraint and the generalized dipole correlation factor are calculated using normal mode analysis. Temperature factors are also computed by normal mode analysis and are in reasonable agreement with those found experimentally. The computed dielectric constant is low; the best estimate is that it falls between 2.5 and 4.
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Cites
Electrostatic recognition between superoxide and copper, zinc superoxide dismutase
Getzoff, E. D., Tainer, J. A., Weiner, P. K., Kollman, P. A., Richardson, J. S., & Richardson, D. C. (1983) · Nature · doi:10.1038/306287a0 · Cited by 554
An external point-charge model for bacteriorhodopsin to account for its purple color
Nakanishi, K., Balogh-Nair, V., Arnaboldi, M., Tsujimoto, K., & Honig, B. (1980) · Journal of the American Chemical Society · doi:10.1021/ja00547a028 · Cited by 327
Self-citation
Cited by
pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model
Bashford, D., & Karplus, M. (1990) · Biochemistry · doi:10.1021/bi00496a010 · Cited by 1,083
On the calculation of p Kas in proteins
Yang, A., Gunner, M. R., Sampogna, R., Sharp, K., & Honig, B. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340150304 · Cited by 508
Self-citationStructure and Mechanisms of F-Type ATP Synthases
Kühlbrandt, W. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110903 · Cited by 444
Sham, Y. Y., Chu, Z. T., & Warshel, A. (1997) · The Journal of Physical Chemistry B · doi:10.1021/jp963412w · Cited by 356
A smooth permittivity function for Poisson–Boltzmann solvation methods
Grant, J. A., Pickup, B. T., & Nicholls, A. (2001) · Journal of Computational Chemistry · doi:10.1002/jcc.1032 · Cited by 340
Metadata
- Authors
- Gilson, M. K., & Honig, B. H.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1986-11
- Volume
- 25
- Issue
- 11
- Pages
- 2097-2119
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2146686098
- Cited by
- 460
- References
- 2
- FWCI
- 1.11
- Type
- journal article
- Language
- en
- Open access
- closed
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- Gilson, M. K., & Honig, B. H. (1986). The dielectric constant of a folded protein. Biopolymers. https://doi.org/10.1002/bip.360251106
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