The 28–111 disulfide bond constrains the α-lactalbumin molten globule and weakens its cooperativity of folding

Eitemau Tebyg

• Hydrophobic sequence minimization of the α-lactalbumin molten globule
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  Cyhoeddwyd: (1997)
• Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bond.
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  Cyhoeddwyd: (1998)
• Pressure-induced unfolding of the molten globule of all-Ala α-lactalbumin
  gan: Lassalle, Michael W., et al.
  Cyhoeddwyd: (2003)
• Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.
  gan: Loh, S N, et al.
  Cyhoeddwyd: (1995)
• Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.
  gan: Kobashigawa, Y., et al.
  Cyhoeddwyd: (1999)