Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme.

@article{Takano2001RoleON,
  title={Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme.},
  author={Keisuke Takano and Yuriko Yamagata and Katsuhide Yutani},
  journal={Proteins},
  year={2001},
  volume={44 3},
  pages={233-43}
}
To understand the role of non-Gly residues in the left-handed helical conformation for the conformational stability of a protein, the non-Gly to Gly and Ala mutations at six left-handed residues (R21, Y38, R50, Q58, H78, and N118) of the human lysozyme were examined. The thermodynamic parameters for denaturation were determined using a differential scanning calorimeter, and the crystal structures were analyzed by X-ray crystallography. If a left-handed non-Gly had an unfavorable steric… CONTINUE READING

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