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228 related items for PubMed ID: 11821052

  • 1. The unfolding mechanism and the disulfide structures of denatured lysozyme.
    Chang JY, Li L.
    FEBS Lett; 2002 Jan 30; 511(1-3):73-8. PubMed ID: 11821052
    [Abstract] [Full Text] [Related]

  • 2. The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin.
    Chang JY, Li L.
    J Biol Chem; 2001 Mar 30; 276(13):9705-12. PubMed ID: 11118458
    [Abstract] [Full Text] [Related]

  • 3. Two-state folding of lysozyme versus multiple-state folding of alpha-lactalbumin illustrated by the technique of disulfide scrambling.
    Li L, Chang JY.
    Protein J; 2004 Jan 30; 23(1):3-10. PubMed ID: 15115177
    [Abstract] [Full Text] [Related]

  • 4. The structure of denatured bovine pancreatic trypsin inhibitor (BPTI).
    Chang J, Ballatore A.
    FEBS Lett; 2000 May 12; 473(2):183-7. PubMed ID: 10812071
    [Abstract] [Full Text] [Related]

  • 5. The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge.
    Yokota A, Izutani K, Takai M, Kubo Y, Noda Y, Koumoto Y, Tachibana H, Segawa S.
    J Mol Biol; 2000 Feb 04; 295(5):1275-88. PubMed ID: 10653703
    [Abstract] [Full Text] [Related]

  • 6. Relationship between the optimal temperature for oxidative refolding and the thermal stability of refolded state of hen lysozyme three-disulfide derivatives.
    Tachibana H, Ohta K, Sawano H, Koumoto Y, Segawa S.
    Biochemistry; 1994 Dec 20; 33(50):15008-16. PubMed ID: 7999758
    [Abstract] [Full Text] [Related]

  • 7. The unfolding pathway and conformational stability of potato carboxypeptidase inhibitor.
    Chang JY, Li L, Canals F, Aviles FX.
    J Biol Chem; 2000 May 12; 275(19):14205-11. PubMed ID: 10799497
    [Abstract] [Full Text] [Related]

  • 8. Kinetics of folding of guanidine-denatured hen egg white lysozyme and carboxymethyl(Cys6,Cys127)-lysozyme: a stopped-flow absorbance and fluorescence study.
    Denton ME, Rothwarf DM, Scheraga HA.
    Biochemistry; 1994 Sep 20; 33(37):11225-36. PubMed ID: 7727374
    [Abstract] [Full Text] [Related]

  • 9. The disulfide structure of denatured epidermal growth factor: preparation of scrambled disulfide isomers.
    Chang JY, Li L.
    J Protein Chem; 2002 Mar 20; 21(3):203-13. PubMed ID: 12018622
    [Abstract] [Full Text] [Related]

  • 10. Investigating conformational stability of bovine pancreatic phospholipase A2: a novel concept in evaluating the contribution of the 'native-framework' of disulphides to the global conformational stability of proteins.
    Singh RR, Chang JY.
    Biochem J; 2004 Feb 01; 377(Pt 3):685-92. PubMed ID: 14533980
    [Abstract] [Full Text] [Related]

  • 11. 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
    [Abstract] [Full Text] [Related]

  • 12. Structural stability of human alpha-thrombin studied by disulfide reduction and scrambling.
    Rajesh Singh R, Chang JY.
    Biochim Biophys Acta; 2003 Sep 23; 1651(1-2):85-92. PubMed ID: 14499592
    [Abstract] [Full Text] [Related]

  • 13. The unfolding pathway of leech carboxypeptidase inhibitor.
    Salamanca S, Villegas V, Vendrell J, Li L, Aviles FX, Chang JY.
    J Biol Chem; 2002 May 17; 277(20):17538-43. PubMed ID: 11893741
    [Abstract] [Full Text] [Related]

  • 14. Evidence for an initiation site for hen lysozyme folding from the reduced form using its dissected peptide fragments.
    Ohkuri T, Ueda T, Tsurumaru M, Imoto T.
    Protein Eng; 2001 Nov 17; 14(11):829-33. PubMed ID: 11742101
    [Abstract] [Full Text] [Related]

  • 15. 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
    [Abstract] [Full Text] [Related]

  • 16. Role of Disulfide Bonds and Topological Frustration in the Kinetic Partitioning of Lysozyme Folding Pathways.
    Muttathukattil AN, Singh PC, Reddy G.
    J Phys Chem B; 2019 Apr 18; 123(15):3232-3241. PubMed ID: 30913878
    [Abstract] [Full Text] [Related]

  • 17. 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]

  • 18. 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]

  • 19. Native-like tertiary structure formation in the alpha-domain of a hen lysozyme two-disulfide variant.
    Tachibana H, Oka T, Akasaka K.
    J Mol Biol; 2001 Nov 23; 314(2):311-20. PubMed ID: 11718564
    [Abstract] [Full Text] [Related]

  • 20. Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers.
    Chang JY.
    J Biol Chem; 1999 Jan 01; 274(1):123-8. PubMed ID: 9867819
    [Abstract] [Full Text] [Related]

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