Article
Enhanced thermodynamic stabilities of yeast iso-1-cytochromes c with amino acid replacements at positions 52 and 102.
The Journal of biological chemistry - 25 Jun 1991
Hickey D R, Berghuis A M, Lafond G, Jaeger J A, Cardillo T S, McLendon D, Das G, Sherman F, Brayer G D, McLendon G
Abstract excerpt
We have determined the structures and thermodynamic stabilities of the wild type Asn-52 and unusually thermostable mutant Ile-52 yeast iso-1-cytochromes c (Das, G., Hickey, D. R. McLendon, D., McLendon, G., and Sherman, F. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 496-499). Although both structures were similar, Water-166, buried within the wild type protein, is excluded from the Ile-52 mutant, which substantially...
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