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Journal Abstract Search

390 related items for PubMed ID: 9761482

  • 1.
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  • 2. Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.
    Kataoka M, Kuwajima K, Tokunaga F, Goto Y.
    Protein Sci; 1997 Feb; 6(2):422-30. PubMed ID: 9041645
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  • 3. 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 Feb; 283(1):265-77. PubMed ID: 9761689
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  • 4. Effects of a helix substitution on the folding mechanism of bovine alpha-lactalbumin.
    Mizuguchi M, Kobashigawa Y, Kumaki Y, Demura M, Kawano K, Nitta K.
    Proteins; 2002 Oct 01; 49(1):95-103. PubMed ID: 12211019
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  • 5. Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A.
    Gast K, Zirwer D, Müller-Frohne M, Damaschun G.
    Protein Sci; 1999 Mar 01; 8(3):625-34. PubMed ID: 10091665
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  • 8. Vibrational Raman optical activity of alpha-lactalbumin: comparison with lysozyme, and evidence for native tertiary folds in molten globule states.
    Wilson G, Ford SJ, Cooper A, Hecht L, Wen ZQ, Barron LD.
    J Mol Biol; 1995 Dec 08; 254(4):747-60. PubMed ID: 7500347
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  • 9. Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin.
    Mizuguchi M, Masaki K, Demura M, Nitta K.
    J Mol Biol; 2000 May 19; 298(5):985-95. PubMed ID: 10801363
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  • 10. 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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  • 11. pH-dependent stability of the human alpha-lactalbumin molten globule state: contrasting roles of the 6 - 120 disulfide and the beta-subdomain at low and neutral pH.
    Horng JC, Demarest SJ, Raleigh DP.
    Proteins; 2003 Aug 01; 52(2):193-202. PubMed ID: 12833543
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  • 12. 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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  • 13. The molten globule protein conformation probed by disulphide bonds.
    Ewbank JJ, Creighton TE.
    Nature; 1991 Apr 11; 350(6318):518-20. PubMed ID: 1901628
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  • 14. Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin.
    Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, Redfield C, Dobson CM.
    J Mol Biol; 1999 May 14; 288(4):673-88. PubMed ID: 10329172
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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 14; 8(12):2765-72. PubMed ID: 10631994
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  • 19. Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states.
    Ikeguchi M, Sugai S, Fujino M, Sugawara T, Kuwajima K.
    Biochemistry; 1992 Dec 22; 31(50):12695-700. PubMed ID: 1472507
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  • 20. Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin.
    Arai M, Kuwajima K.
    Fold Des; 1996 Dec 22; 1(4):275-87. PubMed ID: 9079390
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