BPTI: Protein NMR References

1. Molinari H. Esposito G. Ragona L. Pegna M. Niccolai N. Brunne RM. Lesk AM. Zetta L. Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor. Biophysical Journal. 73(1):382-96, 1997.
   
   
2. Liu Y. Breslauer K. Anderson S. "Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor. Biochemistry. 36(18):5323-35, 1997.
   
   
3. Ma LC. Anderson S. Correlation between disulfide reduction and conformational unfolding in bovine pancreatic trypsin inhibitor. Biochemistry. 36(12):3728-36, 1997.
   
   
4. Ilyina E. Roongta V. Pan H. Woodward C. Mayo KH. A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association. Biochemistry. 36(11):3383-8, 1997.
   
   
5. Christoffersen M. Bolvig S. Tuchsen E. Salt effects on the amide hydrogen exchange of bovine pancreatic trypsin inhibitor. Biochemistry. 35(7):2309-15, 1996.
   
   
6. Kortemme T. Hollecker M. Kemmink J. Creighton TE. Comparison of the (30-51, 14-38) two-disulphide folding intermediates of the homologous proteins dendrotoxin K and bovine pancreatic trypsin inhibitor by two-dimensional ¹H nuclear magnetic resonance. Journal of Molecular Biology. 257(1):188-98, 1996.
   
   
7. Goossens K. Smeller L. Frank J. Heremans K. Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier-transform infrared spectroscopy. European Journal of Biochemistry. 236(1):254-62, 1996.
   
   
8. Chesshyre JA. Kraunsoe JA. Lowe G. Production of bovine-pancreatic-trypsin-inhibitor homologues in Escherichia coli and their characterization. Biotechnology & Applied Biochemistry. 22 ( Pt 3):269-80, 1995.
   
   
9. Brunne RM. Berndt KD. Guntert P. Wuthrich K. van Gunsteren WF. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations. Proteins. 23(1):49-62, 1995.
   
   
10. Pan H. Barbar E. Barany G. Woodward C. Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 34(43):13974-81, 1995.
    
    
11. Dadlez M. Kim PS. A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor. Nature Structural Biology. 2(8):674-9, 1995.
    
    
12. Denisov VP. Halle B. Peters J. Horlein HD. Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant. Biochemistry. 34(28):9046-51, 1995.
    
    
13. Darby NJ. Morin PE. Talbo G. Creighton TE. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates. Journal of Molecular Biology. 249(2):463-77, 1995.
    
    
14. Ferrer M. Barany G. Woodward C. Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor. Nature Structural Biology. 2(3):211-7, 1995.
    
    
15. Ittah V. Haas E. Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor. Biochemistry. 34(13):4493-506, 1995.
    
    
16. Denisov VP. Halle B. Hydrogen exchange and protein hydration: the deuteron spin relaxation dispersions of bovine pancreatic trypsin inhibitor and ubiquitin. Journal of Molecular Biology. 245(5):698-709, 1995.
    
    
17. Denisov VP. Halle B. Protein hydration dynamics in aqueous solution: a comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. Journal of Molecular Biology. 245(5):682-97, 1995.
    
    
18. Staley JP. Kim PS. Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor. Protein Science. 3(10):1822-32, 1994.
    
    
19. Gallagher WH. Croker KM. Identification of a molecular switch that selects between two crystals forms of bovine pancreatic trypsin inhibitor. Protein Science. 3(9):1602-4, 1994.
    
    
20. Lumb KJ. Kim PS. Formation of a hydrophobic cluster in denatured bovine pancreatic trypsin Inhibitor Journal of Molecular Biology. 236(2):412-20, 1994.
    
    
21. van Mierlo CP. Kemmink J. Neuhaus D. Darby NJ. Creighton TE. ¹H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology. 235(3):1044-61, 1994.
    
    
22. Kemmink J. Creighton TE. Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding. Journal of Molecular Biology. 234(3):861-78, 1993.
    
    
23. Hao MH. Pincus MR. Rackovsky S. Scheraga HA. Unfolding and refolding of the native structure of bovine pancreatic trypsin inhibitor studied by computer simulations. Biochemistry. 32(37):9614-31, 1993.
    
    
24. Creighton TE. Bagley CJ. Cooper L. Darby NJ. Freedman RB. Kemmink J. Sheikh A. On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes. Journal of Molecular Biology. 232(4):1176-96, 1993.
    
    
25. Darby NJ. Creighton TE. Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced protein. Journal of Molecular Biology. 232(3):873-96, 1993.
    
    
26. Kim KS. Tao F. Fuchs J. Danishefsky AT. Housset D. Wlodawer A. Woodward C. Crevice-forming mutants of bovine pancreatic trypsin inhibitor: stability changes and new hydrophobic surface. Protein Science. 2(4):588-96, 1993.
    
    
27. Brunne RM. Liepinsh E. Otting G. Wuthrich K. van Gunsteren WF. Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations. Journal of Molecular Biology. 231(4):1040-8, 1993.
    
    
28. Kemmink J. van Mierlo CP. Scheek RM. Creighton TE. Local structure due to an aromatic-amide interaction observed by ¹H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology.230(1):312-22, 1993.
    
    
29. van Mierlo CP. Darby NJ. Keeler J. Neuhaus D. Creighton TE. Partially folded conformation folding pathway of bovine pancreatic trypsin inhibitor. ¹H and ¹⁵N resonance of the (30-51) intermediate in the disulphide assignments and determination of backbone dynamics from ¹⁵N relaxation measurements. Journal of Molecular Biology. 229(4):1125-46, 1993.
    
    
30. Danishefsky AT. Housset D. Kim KS. Tao F. Fuchs J. Woodward C. Wlodawer A. Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A. Protein Science. 2(4):577-87, 1993.