1qcv
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qcv OCA], [http://www.ebi.ac.uk/pdbsum/1qcv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qcv RCSB]</span> | ||
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[[Category: rubredoxin]] | [[Category: rubredoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:57 2008'' |
Revision as of 20:11, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON
Overview
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.
About this Structure
1QCV is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Contribution of surface salt bridges to protein stability., Strop P, Mayo SL, Biochemistry. 2000 Feb 15;39(6):1251-5. PMID:10684603
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