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183 related items for PubMed ID: 2454656

  • 1. Kinetic analysis of the folding and unfolding of a mutant form of bovine pancreatic trypsin inhibitor lacking the cysteine-14 and -38 thiols.
    Goldenberg DP.
    Biochemistry; 1988 Apr 05; 27(7):2481-9. PubMed ID: 2454656
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 3. Disulfide bond-coupled folding of bovine pancreatic trypsin inhibitor derivatives missing one or two disulfide bonds.
    Kosen PA, Marks CB, Falick AM, Anderson S, Kuntz ID.
    Biochemistry; 1992 Jun 30; 31(25):5705-17. PubMed ID: 1377024
    [Abstract] [Full Text] [Related]

  • 4. Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds.
    Hurle MR, Marks CB, Kosen PA, Anderson S, Kuntz ID.
    Biochemistry; 1990 May 08; 29(18):4410-9. PubMed ID: 1693524
    [Abstract] [Full Text] [Related]

  • 5. Early events in the disulfide-coupled folding of BPTI.
    Bulaj G, Goldenberg DP.
    Protein Sci; 1999 Sep 08; 8(9):1825-42. PubMed ID: 10493584
    [Abstract] [Full Text] [Related]

  • 6. Mutational analysis of hydrogen bonding residues in the BPTI folding pathway.
    Bulaj G, Goldenberg DP.
    J Mol Biol; 2001 Oct 26; 313(3):639-56. PubMed ID: 11676545
    [Abstract] [Full Text] [Related]

  • 7. Mutants of bovine pancreatic trypsin inhibitor lacking cysteines 14 and 38 can fold properly.
    Marks CB, Naderi H, Kosen PA, Kuntz ID, Anderson S.
    Science; 1987 Mar 13; 235(4794):1370-3. PubMed ID: 2435002
    [Abstract] [Full Text] [Related]

  • 8. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates.
    Darby NJ, Morin PE, Talbo G, Creighton TE.
    J Mol Biol; 1995 Jun 02; 249(2):463-77. PubMed ID: 7540214
    [Abstract] [Full Text] [Related]

  • 9. "Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor.
    Liu Y, Breslauer K, Anderson S.
    Biochemistry; 1997 May 06; 36(18):5323-35. PubMed ID: 9154914
    [Abstract] [Full Text] [Related]

  • 10. Effects of amino acid replacements on the reductive unfolding kinetics of pancreatic trypsin inhibitor.
    Mendoza JA, Jarstfer MB, Goldenberg DP.
    Biochemistry; 1994 Feb 08; 33(5):1143-8. PubMed ID: 7509189
    [Abstract] [Full Text] [Related]

  • 11. Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine beta-trypsin.
    Krokoszynska I, Dadlez M, Otlewski J.
    J Mol Biol; 1998 Jan 23; 275(3):503-13. PubMed ID: 9466927
    [Abstract] [Full Text] [Related]

  • 12. Amino acid replacement that eliminates kinetic traps in the folding pathway of pancreatic trypsin inhibitor.
    Zhang JX, Goldenberg DP.
    Biochemistry; 1993 Dec 28; 32(51):14075-81. PubMed ID: 7505111
    [Abstract] [Full Text] [Related]

  • 13. Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.
    Zapun A, Creighton TE.
    Biochemistry; 1994 May 03; 33(17):5202-11. PubMed ID: 7513556
    [Abstract] [Full Text] [Related]

  • 14. Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation.
    Bulaj G, Koehn RE, Goldenberg DP.
    Protein Sci; 2004 May 03; 13(5):1182-96. PubMed ID: 15096625
    [Abstract] [Full Text] [Related]

  • 15. Native-like interactions favored in the unfolded bovine pancreatic trypsin inhibitor have different roles in folding.
    Li R, Battiste JL, Woodward C.
    Biochemistry; 2002 Feb 19; 41(7):2246-53. PubMed ID: 11841216
    [Abstract] [Full Text] [Related]

  • 16. Hydrophobic interactions accelerate early stages of the folding of BPTI.
    Dadlez M.
    Biochemistry; 1997 Mar 11; 36(10):2788-97. PubMed ID: 9062106
    [Abstract] [Full Text] [Related]

  • 17. Phi-values for BPTI folding intermediates and implications for transition state analysis.
    Bulaj G, Goldenberg DP.
    Nat Struct Biol; 2001 Apr 11; 8(4):326-30. PubMed ID: 11276252
    [Abstract] [Full Text] [Related]

  • 18. Unfolding and refolding of the native structure of bovine pancreatic trypsin inhibitor studied by computer simulations.
    Hao MH, Pincus MR, Rackovsky S, Scheraga HA.
    Biochemistry; 1993 Sep 21; 32(37):9614-31. PubMed ID: 7690589
    [Abstract] [Full Text] [Related]

  • 19. Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability.
    Kowalski JM, Parekh RN, Wittrup KD.
    Biochemistry; 1998 Feb 03; 37(5):1264-73. PubMed ID: 9477952
    [Abstract] [Full Text] [Related]

  • 20. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor.
    Weissman JS, Kim PS.
    Proc Natl Acad Sci U S A; 1992 Oct 15; 89(20):9900-4. PubMed ID: 1384063
    [Abstract] [Full Text] [Related]

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