Side-chain conformational disorder in a molten globule: molecular dynamics simulations of the A-state of human α-lactalbumin

This publication has 36 references indexed in Scilit:

• Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
  Folding and Design, 1996
• Sequence space, folding and protein design
  Current Opinion in Structural Biology, 1996
• Following protein folding in real time using NMR spectroscopy
  Nature Structural & Molecular Biology, 1995
• Protein Folding: Solid evidence for molten globules
  Current Biology, 1994
• De novo protein design: from molten globules to native-like states
  Current Opinion in Structural Biology, 1993
• Molecular simulations of peptide and protein unfolding: in quest of a molten globule
  Current Opinion in Structural Biology, 1993
• ¹H‐NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of α‐lactalbumin
  European Journal of Biochemistry, 1992
• Crystal structure of human α-lactalbumin at 1·7 Å resolution
  Journal of Molecular Biology, 1991
• Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin
  Biochemistry, 1989
• Molecular dynamics with coupling to an external bath
  The Journal of Chemical Physics, 1984