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Contribution of surface salt bridges to protein stability

Strop, Pavel and Mayo, Stephen L. (2000) Contribution of surface salt bridges to protein stability. Biochemistry, 39 (6). pp. 1251-1255. ISSN 0006-2960. doi:10.1021/bi992257j.

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The role of surface salt bridges in protein stabilization has been a source of controversy. Here we present the NMR structure of a hyperthermophilic rubredoxin variant (PFRD-XC4) and the thermodynamic analysis of two surface salt bridges by double mutant cycles. This analysis shows that the surface side chain to side chain salt bridge between Lys 6 and Glu 49 does not stabilize PFRD-XC4. The main chain to side chain salt bridge between the N-terminus and Glu 14 was, however, found to stabilize PFRD-XC4 by 1. 5 kcal mol^(-1). The entropic cost of making a surface salt bridge involving the protein's backbone is reduced, since the backbone has already been immobilized upon protein folding.

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Mayo, Stephen L.0000-0002-9785-5018
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Additional Information:© 2000 American Chemical Society. Received September 27, 1999; Revised Manuscript Received November 16, 1999. Published on Web 01/19/2000. This work was supported by the Howard Huges Medical Institute (S.L.M.) and a NSF fellowship (P.S.). The coordinates for the structure have been deposited in the Protein Data Bank (file 1qcv). We thank M. K. Eidsness for the wild-type P. furiosus rubredoxin gene used in this study, S. Ross for NMR spectroscopy, and S. Ross and C. Sarisky for help with the NMR structure determination.
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Howard Hughes Medical Institute (HHMI)UNSPECIFIED
NSF Graduate Research FellowshipUNSPECIFIED
Subject Keywords:Solvents; Bacterial Proteins; Hydrogen Bonding; Solutions; Mutagenesis: Site-Directed; Pyrococcus furiosus; Crystallography: X-Ray; Protein Denaturation; Nuclear Magnetic Resonance: Biomolecular; Rubredoxins; Salts; Thermodynamics; Guanidine
Issue or Number:6
Record Number:CaltechAUTHORS:20110620-160425030
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Official Citation:Contribution of Surface Salt Bridges to Protein Stability, Pavel Strop and Stephen L. Mayo, Biochemistry 2000 39 (6), 1251-1255
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:24083
Deposited By: Marie Ary
Deposited On:28 Sep 2011 22:26
Last Modified:09 Nov 2021 16:20

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