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257 related items for PubMed ID: 12484765

  • 1. Insight into the factors influencing the backbone dynamics of three homologous proteins, dendrotoxins I and K, and BPTI: FTIR and time-resolved fluorescence investigations.
    Hollecker M, Vincent M, Gallay J, Ruysschaert JM, Goormaghtigh E.
    Biochemistry; 2002 Dec 24; 41(51):15267-76. PubMed ID: 12484765
    [Abstract] [Full Text] [Related]

  • 2. Molecular structure, conformational analysis, and structure-activity studies of Dendrotoxin and its homologues using molecular mechanics and molecular dynamics techniques.
    Swaminathan P, Hariharan M, Murali R, Singh CU.
    J Med Chem; 1996 May 24; 39(11):2141-55. PubMed ID: 8667358
    [Abstract] [Full Text] [Related]

  • 3. A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility.
    Battiste JL, Li R, Woodward C.
    Biochemistry; 2002 Feb 19; 41(7):2237-45. PubMed ID: 11841215
    [Abstract] [Full Text] [Related]

  • 4. Hydrogen exchange in BPTI variants that do not share a common disulfide bond.
    Schulman BA, Kim PS.
    Protein Sci; 1994 Dec 19; 3(12):2226-32. PubMed ID: 7538845
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  • 5. Dynamics of the conformational ensemble of partially folded bovine pancreatic trypsin inhibitor.
    Barbar E, Hare M, Daragan V, Barany G, Woodward C.
    Biochemistry; 1998 May 26; 37(21):7822-33. PubMed ID: 9601043
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  • 6. Conformational and functional variability supported by the BPTI fold: solution structure of the Ca2+ channel blocker calcicludine.
    Gilquin B, Lecoq A, Desné F, Guenneugues M, Zinn-Justin S, Ménez A.
    Proteins; 1999 Mar 01; 34(4):520-32. PubMed ID: 10081964
    [Abstract] [Full Text] [Related]

  • 7. Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy.
    Takeda N, Nakano K, Kato M, Taniguchi Y.
    Biospectroscopy; 1998 Mar 01; 4(3):209-16. PubMed ID: 9639111
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  • 8. Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.
    Roder H, Wagner G, Wüthrich K.
    Biochemistry; 1985 Dec 03; 24(25):7396-407. PubMed ID: 2417625
    [Abstract] [Full Text] [Related]

  • 9. Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor.
    Brandt P, Woodward C.
    Biochemistry; 1987 Jun 02; 26(11):3156-67. PubMed ID: 2440473
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  • 13. Accelerated exchange of a buried water molecule in selectively disulfide-reduced bovine pancreatic trypsin inhibitor.
    Denisov VP, Peters J, Hörlein HD, Halle B.
    Biochemistry; 2004 Sep 28; 43(38):12020-7. PubMed ID: 15379542
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  • 15. Hydrophobic interactions accelerate early stages of the folding of BPTI.
    Dadlez M.
    Biochemistry; 1997 Mar 11; 36(10):2788-97. PubMed ID: 9062106
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  • 16. Selective bridging of bis-cysteinyl residues by arsonous acid derivatives as an approach to the characterization of protein tertiary structures and folding pathways by mass spectrometry.
    Happersberger HP, Przybylski M, Glocker MO.
    Anal Biochem; 1998 Nov 15; 264(2):237-50. PubMed ID: 9866689
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  • 17. Determinants of backbone dynamics in native BPTI: cooperative influence of the 14-38 disulfide and the Tyr35 side-chain.
    Beeser SA, Oas TG, Goldenberg DP.
    J Mol Biol; 1998 Dec 18; 284(5):1581-96. PubMed ID: 9878372
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  • 18. Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation.
    Bulaj G, Koehn RE, Goldenberg DP.
    Protein Sci; 2004 May 18; 13(5):1182-96. PubMed ID: 15096625
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  • 19. Protein internal flexibility and global stability: effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor.
    Kim KS, Woodward C.
    Biochemistry; 1993 Sep 21; 32(37):9609-13. PubMed ID: 7690588
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