Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants.

@article{Yamagata1998ContributionOH,
  title={Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants.},
  author={Yuriko Yamagata and Michio Kubota and Yasuyuki Sumikawa and Jun Funahashi and Kazufumi Takano and Satoshi Fujii and Katsuhide Yutani},
  journal={Biochemistry},
  year={1998},
  volume={37 26},
  pages={9355-62}
}
The contribution of hydrogen bonds to the conformational stability of human lysozyme was investigated by the combination of calorimetric and X-ray analyses of six Tyr --> Phe mutants. Unfolding Delta G and unfolding Delta H values of the Tyr --> Phe mutant proteins were changed by from +0.3 to -4.0 kJ/mol and from 0 to -16 kJ/mol, respectively, compared to those of the wild-type protein. The net contribution of a hydrogen bond at a specific site to stability (Delta Gwild/HB), considering… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.

Similar Papers

Loading similar papers…