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Journal Abstract Search

1029 related items for PubMed ID: 15641801

  • 1. 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
    [Abstract] [Full Text] [Related]

  • 2. Evidence for the underlying cause of diversity of the disulfide folding pathway.
    Chang JY.
    Biochemistry; 2004 Apr 20; 43(15):4522-9. PubMed ID: 15078098
    [Abstract] [Full Text] [Related]

  • 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 Apr 20; 283(1):265-77. PubMed ID: 9761689
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  • 4. Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme.
    Bai P, Peng Z.
    J Mol Biol; 2001 Nov 23; 314(2):321-9. PubMed ID: 11718563
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  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy.
    Kuwajima K, Yamaya H, Sugai S.
    J Mol Biol; 1996 Dec 13; 264(4):806-22. PubMed ID: 8980687
    [Abstract] [Full Text] [Related]

  • 7. Hierarchical unfolding of the alpha-lactalbumin molten globule: presence of a compact intermediate without a unique tertiary fold.
    Chakraborty S, Peng Z.
    J Mol Biol; 2000 Apr 21; 298(1):1-6. PubMed ID: 10756101
    [Abstract] [Full Text] [Related]

  • 8. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
    Patra AK, Udgaonkar JB.
    Biochemistry; 2007 Oct 23; 46(42):11727-43. PubMed ID: 17902706
    [Abstract] [Full Text] [Related]

  • 9. Pathway of oxidative folding of a 3-disulfide alpha-lactalbumin may resemble either BPTI model or hirudin model.
    Salamanca S, Chang JY.
    Protein J; 2006 Jun 23; 25(4):275-87. PubMed ID: 16710754
    [Abstract] [Full Text] [Related]

  • 10. Cold denaturation of alpha-lactalbumin.
    Mizuguchi M, Hashimoto D, Sakurai M, Nitta K.
    Proteins; 2000 Mar 01; 38(4):407-13. PubMed ID: 10707027
    [Abstract] [Full Text] [Related]

  • 11. Molten globule of bovine alpha-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis.
    Polverino de Laureto P, Frare E, Gottardo R, Fontana A.
    Proteins; 2002 Nov 15; 49(3):385-97. PubMed ID: 12360528
    [Abstract] [Full Text] [Related]

  • 12. Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling.
    Lewney S, Smith LJ.
    Proteins; 2012 Mar 15; 80(3):913-9. PubMed ID: 22189830
    [Abstract] [Full Text] [Related]

  • 13. Energetic basis of structural stability in the molten globule state: alpha-lactalbumin.
    Griko YV.
    J Mol Biol; 2000 Apr 14; 297(5):1259-68. PubMed ID: 10764588
    [Abstract] [Full Text] [Related]

  • 14. Compactness of the kinetic molten globule of bovine alpha-lactalbumin: a dynamic light scattering study.
    Gast K, Zirwer D, Müller-Frohne M, Damaschun G.
    Protein Sci; 1998 Sep 14; 7(9):2004-11. PubMed ID: 9761482
    [Abstract] [Full Text] [Related]

  • 15. Correlation between disulfide reduction and conformational unfolding in bovine pancreatic trypsin inhibitor.
    Ma LC, Anderson S.
    Biochemistry; 1997 Mar 25; 36(12):3728-36. PubMed ID: 9132026
    [Abstract] [Full Text] [Related]

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  • 19. The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling. Isolation of on-pathway and off-pathway intermediates.
    Chang JY.
    J Biol Chem; 2002 Jan 04; 277(1):120-6. PubMed ID: 11560938
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