Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease.

@article{Shortle1990ContributionsOT,
  title={Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease.},
  author={David Shortle and Wesley E. Stites and Alan K Meeker},
  journal={Biochemistry},
  year={1990},
  volume={29 35},
  pages={8033-41}
}
To quantitate the contributions of the large hydrophobic residues in staphylococcal nuclease to the stability of its native state, single alanine and glycine substitutions were constructed by site-directed mutagenesis for each of the 11 leucine, 9 valine, 7 tyrosine, 5 isoleucine, 4 methionine, and 3 phenylalanine residues. In addition, each isoleucine was also mutated to valine. The resulting collection of 83 mutant nucleases was submitted to guanidine hydrochloride denaturation using… CONTINUE READING
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The Hydrophobic Effect

  • C. Tanford
  • Adu. Protein Chem
  • 1980
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