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1697 related items for PubMed ID: 9761689

  • 1. Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.
    Mizuguchi M, Arai M, Ke Y, Nitta K, Kuwajima K.
    J Mol Biol; 1998; 283(1):265-77. PubMed ID: 9761689
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  • 3. Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions.
    Sasahara K, Demura M, Nitta K.
    Proteins; 2002 Dec 01; 49(4):472-82. PubMed ID: 12402357
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  • 7. Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism.
    Nakao M, Maki K, Arai M, Koshiba T, Nitta K, Kuwajima K.
    Biochemistry; 2005 May 03; 44(17):6685-92. PubMed ID: 15850402
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  • 8. Cold denaturation of alpha-lactalbumin.
    Mizuguchi M, Hashimoto D, Sakurai M, Nitta K.
    Proteins; 2000 Mar 01; 38(4):407-13. PubMed ID: 10707027
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  • 10. Hexafluoroacetone hydrate as a structure modifier in proteins: characterization of a molten globule state of hen egg-white lysozyme.
    Bhattacharjya S, Balaram P.
    Protein Sci; 1997 May 01; 6(5):1065-73. PubMed ID: 9144778
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  • 14. Unfolding and refolding pathways of a major kinetic trap in the oxidative folding of alpha-lactalbumin.
    Salamanca S, Chang JY.
    Biochemistry; 2005 Jan 18; 44(2):744-50. PubMed ID: 15641801
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  • 17. Kinetics of folding and unfolding of goat alpha-lactalbumin.
    Chedad A, Van Dael H.
    Proteins; 2004 Nov 01; 57(2):345-56. PubMed ID: 15340922
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  • 18. Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.
    Kobashigawa Y, Sakurai M, Nitta K.
    Protein Sci; 1999 Dec 01; 8(12):2765-72. PubMed ID: 10631994
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