NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.

@article{Yokota2004NMRCO,
  title={NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.},
  author={Atsushi Yokota and Kenichi Hirai and Hiroyo Miyauchi and Satoshi Iimura and Yasuo Noda and Kyoko Inoue and Kazuyuki Akasaka and H. Tachibana and Shin-ichi Segawa},
  journal={Biochemistry},
  year={2004},
  volume={43 21},
  pages={6663-9}
}
Our earlier NMR study showed that a two-disulfide variant of hen lysozyme containing intra-alpha-domain disulfide bridges, C6-C127 and C30-C115, is partially folded, with the alpha domain tightly folded to the nativelike conformation and the beta domain flexible or unfolded. With a view that the formation of a third disulfide bridge is a key for the accomplishment of the overall chain fold, three-dimensional structures of three-disulfide variants of hen lysozyme lacking one disulfide bridge… CONTINUE READING

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