Enhanced thermodynamic stabilities of yeast iso-1-cytochromes c with amino acid replacements at positions 52 and 102.

@article{Hickey1991EnhancedTS,
  title={Enhanced thermodynamic stabilities of yeast iso-1-cytochromes c with amino acid replacements at positions 52 and 102.},
  author={D R Hickey and Albert M Berghuis and Gilles Lafond and J A Jaeger and Thomas S Cardillo and David M. McLendon and Goutam Das and Fred Sherman and Gary D. Brayer and George L. McLendon},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 18},
  pages={11686-94}
}
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 reorganizes the local hydrogen bonding. Wild type Cys-102 was replaced with… CONTINUE READING
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