Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface.

@article{Pielak1995ProteinTD,
  title={Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface.},
  author={Gary J Pielak and David S. Auld and James R Beasley and Stephen F. Betz and D. S. Cohen and Donald Francis Doyle and S. Alison Finger and Zoey Fredericks and S Hilgen-Willis and Aleister J Saunders},
  journal={Biochemistry},
  year={1995},
  volume={34 10},
  pages={3268-76}
}
Random mutant libraries with substitutions at the interface between the N- and C-terminal helices of Saccharomyces cerevisiae iso-1-cytochrome c were screened. All residue combinations that have been identified in naturally occurring cytochrome c sequences are found in the libraries. Mutants with these combinations are biologically functional. Enthalpies, heat capacities, and midpoint temperatures of denaturation are used to determine the entropy and Gibbs free energy of denaturation (delta GD… CONTINUE READING

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