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Journal Abstract Search

128 related items for PubMed ID: 10891073

  • 21. High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence.
    Czapinska H, Otlewski J, Krzywda S, Sheldrick GM, Jaskólski M.
    J Mol Biol; 2000 Feb 04; 295(5):1237-49. PubMed ID: 10653700
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  • 22. Formation of a hydrophobic cluster in denatured bovine pancreatic trypsin inhibitor.
    Lumb KJ, Kim PS.
    J Mol Biol; 1994 Feb 18; 236(2):412-20. PubMed ID: 7508987
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  • 24. Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor.
    Pan H, Barany G, Woodward C.
    Protein Sci; 1997 Sep 18; 6(9):1985-92. PubMed ID: 9300498
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  • 25. Native-like conformations are sampled by partially folded and disordered variants of bovine pancreatic trypsin inhibitor.
    Tulla-Puche J, Getun IV, Woodward C, Barany G.
    Biochemistry; 2004 Feb 17; 43(6):1591-8. PubMed ID: 14769035
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  • 27. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
    Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ.
    Biochemistry; 2001 Mar 27; 40(12):3561-71. PubMed ID: 11297422
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  • 28. Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy.
    Takeda N, Nakano K, Kato M, Taniguchi Y.
    Biospectroscopy; 1998 Mar 27; 4(3):209-16. PubMed ID: 9639111
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  • 30. Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor.
    Ittah V, Haas E.
    Biochemistry; 1995 Apr 04; 34(13):4493-506. PubMed ID: 7535565
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  • 31. Folding of bovine pancreatic trypsin inhibitor (BPTI) variants in which almost half the residues are alanine.
    Kuroda Y, Kim PS.
    J Mol Biol; 2000 May 05; 298(3):493-501. PubMed ID: 10772865
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  • 34. 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
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  • 35. Dynamic modelling of a helical peptide in solution using NMR data: multiple conformations and multi-spin effects.
    Kemmink J, Scheek RM.
    J Biomol NMR; 1995 Jul 19; 6(1):33-40. PubMed ID: 7545042
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  • 36. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.
    van Mierlo CP, Darby NJ, Creighton TE.
    Proc Natl Acad Sci U S A; 1992 Aug 01; 89(15):6775-9. PubMed ID: 1379719
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  • 37. Elucidation of the origin of multiple conformations of the human alpha 3-chain type VI collagen C-terminal Kunitz domain: the reorientation of the Trp21 ring.
    Sørensen MD, Kristensen SM, Bjørn S, Norris K, Olsen O, Led JJ.
    J Biomol NMR; 1996 Dec 01; 8(4):391-403. PubMed ID: 9008360
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  • 38. Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stability.
    Ferrer M, Woodward C, Barany G.
    Int J Pept Protein Res; 1992 Dec 01; 40(3-4):194-207. PubMed ID: 1282503
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  • 39. Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution.
    Chazin WJ, Goldenberg DP, Creighton TE, Wüthrich K.
    Eur J Biochem; 1985 Oct 15; 152(2):429-37. PubMed ID: 2414103
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  • 40. 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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