Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state.

@article{Uchiyama1995EffectsOA,
  title={Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state.},
  author={Hirokuni Uchiyama and Eva Perez-Prat and Katsumi Watanabe and Izumi Kumagai and Kunihiro Kuwajima},
  journal={Protein engineering},
  year={1995},
  volume={8 11},
  pages={
          1153-61
        }
}
Five mutant alpha-lactalbumins, with one or two amino acid substitution(s) in the B helix, were engineered to examine the relation between the stability of the molten globule state and the hydrophobicity of these amino acids. The mutation sites (Thr29, Ala30 and Thr33) have been chosen on the basis of comparison of the amino acid sequences of goat, bovine and gunea pig alpha-lactalbumin, in which the guinea pig protein shows a remarkably more stable molten globule than the other proteins. The… CONTINUE READING
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Defining the core structure of the alpha-lactalbumin molten globule state.

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