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Experimental Evaluation of the Effective Dielectric Constant of Proteins

Rees, Douglas C. (1980) Experimental Evaluation of the Effective Dielectric Constant of Proteins. Journal of Molecular Biology, 141 (3). pp. 323-326. ISSN 0022-2836. doi:10.1016/0022-2836(80)90184-9.

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Chemical modifications that alter the net charge of residues in reduction-oxidation proteins influence the redox potential of the protein by changing the electrostatic potential at the redox center. If the locations of the modified charges are known, the shift in redox potential may be used to determine the effective dielectric constant for the interactions between the redox center and modified residues. From the shift in redox potential upon charge neutralization of specific lysines in the hemoprotein cytochrome c, an effective dielectric constant of approximately 50 is calculated for the electrostatic interaction between the modified lysines and heme iron in the native protein.

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Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 1979 Academic Press Inc. (London) Ltd. Received 25 March 1980. We thank W. N. Lipscomb for advice and encouragement. This work was supported by National Institutes of Health grant GM06920.
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Issue or Number:3
Record Number:CaltechAUTHORS:20150210-100445875
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Official Citation:Douglas C. Rees, Experimental evaluation of the effective dielectric constant of proteins, Journal of Molecular Biology, Volume 141, Issue 3, 15 August 1980, Pages 323-326, ISSN 0022-2836, (
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54656
Deposited By: SWORD User
Deposited On:10 Feb 2015 18:11
Last Modified:10 Nov 2021 20:36

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