Contribution of hydrogen bonding to the conformational stability of ribonuclease T1.

@article{Shirley1992ContributionOH,
  title={Contribution of hydrogen bonding to the conformational stability of ribonuclease T1.},
  author={Bret A Shirley and Patrick E. Stanssens and Ulrich Hahn and C. Nick Pace},
  journal={Biochemistry},
  year={1992},
  volume={31 3},
  pages={725-32}
}
For 30 years, the prevailing view has been that the hydrophobic effect contributes considerably more than hydrogen bonding to the conformational stability of globular proteins. The results and reasoning presented here suggest that hydrogen bonding and the hydrophobic effect make comparable contributions to the conformational stability of ribonuclease T1 (RNase T1). When RNase T1 folds, 86 intramolecular hydrogen bonds with an average length of 2.95 A are formed. Twelve mutants of RNase T1 [Tyr… CONTINUE READING

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