Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry.

@article{Connelly1990ThermodynamicsOP,
  title={Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry.},
  author={Patrick R. Connelly and Raghavan Varadarajan and Julian M. Sturtevant and Frederic M. Richards},
  journal={Biochemistry},
  year={1990},
  volume={29 25},
  pages={6108-14}
}
Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex designated ribonuclease S. Residue 13 in the peptide is methionine. According to the X-ray structure of the complex of S-protein and S-peptide (1-20), this residue is almost fully buried. We have substituted Met-13 with seven other hydrophobic residues ranging in size from glycine to phenylalanine and have determined the… CONTINUE READING

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