The native-like tertiary fold in molten globule alpha-lactalbumin appears to be controlled by a continuous phase transition. Journal of Molecular Biology 261(3): 341-347, 1996
Hierarchical unfolding of the a-lactalbumin molten globule: presence of a compact intermediate without a unique tertiary fold. Journal of Molecular Biology 298(1): 6, 2000
Determinants of the native-like tertiary topology in the alpha-lactalbumin molten globule. Kuwajima, Kunihiro Author, Arai, Munehito Author International Congress Series; Old and new views of protein folding 145-154, 1999
Hierarchical unfolding of the alpha-lactalbumin molten globule: presence of a compact intermediate without a unique tertiary fold. Journal of Molecular Biology 298(1): 1-6, 2000
Does the molten globule have a native-like tertiary fold?. Philosophical Transactions of the Royal Society of London. Series B Biological Sciences 348(1323): 43-47, 1995
Contribution of individual residues to formation of the native-like tertiary topology in the a-lactalbumin molten globule. Journal of Molecular Biology 280(1): 7-74, 1998
Non two-state denaturing transition from native to molten globule states of apo-alpha-lactalbumin. Biophysical Journal 72(2 Part 2): A394, 1997
Protein Folding || Does the Molten Globule have a Native-Like Tertiary Fold?. Philosophical Transactions Biological Sciences 348(1323): 43-47, 1995
Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule. Journal of Molecular Biology 280(1): 167-174, 1998
Vibrational Raman optical activity of a-lactalbumin: comparison with lysozyme, and evidence for native tertiary folds in molten globule states. Journal of Molecular Biology 254: 7-60, 1995
Vibrational Raman optical activity of alpha-lactalbumin: comparison with lysozyme, and evidence for native tertiary folds in molten globule states. Journal of Molecular Biology 254(4): 747-760, 1995
Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule?. Biophysical Journal 95(4): 1913-1927, 2008
Direct measurement of the energetics of the molten globule and native states of alpha lactalbumin. Biophysical Journal 61(2 Part 2): A477, 1992
Action of protein-glutaminase on alpha-lactalbumin in the native and molten globule states. Journal of Agricultural and Food Chemistry 49(12): 5999-6005, 2001
Contribution of the 6-120 disulfide bond of a-lactalbumin to the stabilities of its native and molten globule states. Biochemistry (American Chemical Society) 31: 695-700, 1992