Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine β-lactoglobulin

@inproceedings{Yamada2006StructuralAT,
  title={Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine β-lactoglobulin},
  author={Yoshiteru Yamada and Kanako Nakagawa and Takeo Yajima and Keiko Saito and Akihito Tokushima and Kazuo Fujiwara and Masamichi Ikeguchi},
  year={2006}
}
A disulfide bond between cysteine 66 and cysteine 160 of equine β-lactoglobulin was removed by substituting cysteine residues with alanine. This disulfide bond is conserved across the lipocalin family. The conformation and stability of the disulfide-deleted mutant protein was investigated by circular dichroism. The mutant protein assumes a native-like structure under physiological conditions and assumes a helix-rich molten globule structure at acid pH or at moderate concentrations of urea as… CONTINUE READING

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