Contribution of surface salt bridges to protein stability
- Creators
- Strop, Pavel
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Mayo, Stephen L.
Abstract
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.
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.Attached Files
Accepted Version - Strop_2000_Biochemistry_Contribution_of_surface_salt_bridges.pdf
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Additional details
- Eprint ID
- 24083
- Resolver ID
- CaltechAUTHORS:20110620-160425030
- Howard Hughes Medical Institute (HHMI)
- NSF Graduate Research Fellowship
- Created
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2011-09-28Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field