Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink

Folding and Design

Volumn 1, Issue 1, 1996, Pages 65-76

  Barbar, Elisar ^a   Barany, George ^b   Woodward, Clare ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b University of Minnesota   (United States)

Author keywords

BPTI; Denatured states; Disulfide bonds; NMR; Protein folding

Indexed keywords

APROTININ; DISULFIDE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; GENETIC VARIABILITY; GENETICS; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; SYNTHESIS;

AMINO ACID SEQUENCE; ANIMALS; APROTININ; CATTLE; CIRCULAR DICHROISM; DISULFIDES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; VARIATION (GENETICS);

EID: 0030342680     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00013-2     Document Type: Article

References (35)

1. Pan, H., Barbar, E., Barany G. & Woodward, K. (1995). Extensive non-random structure in reduced and unfolded bovine pancreatic trypsin inhibitor. Biochemistry 34, 13974-13981.
2. Barbar, E., Barany, G. & Woodward, C. (1995). Dynamic structure of a highly ordered β-sheet molten globule: multiple conformations with a stable core. Biochemistry 34, 11423-11434.
3. Dill, K. & Shortle, D. (1991). Denatured states of proteins. Annu. Rev. Biochem. 60, 795-825.
4. Shortle, D. (1996). Structural analysis of non-native states of proteins by NMR methods. Curr. Opin. Struct. Biol. in press.
5. Ferrer, M., Barany, G. & Woodward, C. (1995). Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor. Nature Struct. Biol. 2, 211-218.
6. Amir, D., Krausz, S. & Haas, E. (1992). Detection of local structures in reduced unfolded bovine pancreatic trypsin inhibitor. Proteins 13, 162-173.
7. Utah, V. & Haas, E. (1995). Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor Biochemistry 34, 4493-4506.
8. Logan, T., Theriault, Y. & Fesik, S. (1994). Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride. J. Mol. Biol. 236, 637-648.
9. Zhang, O. & Forman-Kay, J. (1995). Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer. Biochemistry 34, 6784-6794 .
10. Kim, K.S., Fuchs, F. & Woodward, C. (1993). Hydrogen exchange identifies native-state motional domains important in protein folding. Biochemistry 32, 9600-9608.
11. Woodward, C. (1993). Is the slow exchange core the folding core? Trends Biochem. Sci. 18, 359-360.
12. Dill, K., Rebig, K. & Chan, H. (1993). Cooperativity in protein-folding kinetics. Proc. Natl. Acad. Sci. U.S.A. 90, 1942-1946.
13. Barany, G., Gross, C.M., Ferrer, M., Barbar, E., Pan, H. & Woodward, K. (1995). Optimized methods for chemical synthesis of bovine pancreatic trysin inhibitor analogues. In Techniques in Protein Chemistry. VII (Marshak, D., ed), Academic Press, San Diego, in press.
14. Kemmink, J. & Creighton, T. (1993). Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding. J. Mol. Biol. 234, 861-878.
15. 1H resonance of Gly37 in BPTI. Biochemistry 26, 1918-1925.
16. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. Wiley and Sons, New York.
17. 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects. J. Biomol. NMR 5, 67-81.
18. Wishart, D.S., Sykes, B.D. & Richards, F.M. (1991). Relationship between nuclear magnetic resonance chemical shifts and protein secondary structure. J. Mol. Biol. 222, 311-333.
19. 1H nuclear magnetic resonance study of the (5-55) single-disulfide folding intermediate of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 222, 373-390.
20. Van Mierlo, C., Darby, N., Keeler, J., Neuhaus, D. & Creighton, T. (1993). Partially folded conformation of the (30-51) intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 229, 1125-1146.
21. Staley, J. & Kim, P. (1992). Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond. Proc. Natl. Acad. Sci. U.S.A. 89, 1519-1523.
22. Staley, J.P. & Kim, P.S. (1994). Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor. Protein Sci. 3, 1822-1832.
23. Creighton, T. (1992). Folding Pathways Determined using Disulfide Bonds in Protein Folding. (Creighton, T., ed.), pp. 301-351, W.H. Freeman & Co., New York.
24. Weissman, J.S. & Kim, P.S. (1991). Reexamination of the folding of BPTI: predominance of native intermediates. Science 253, 1386-1393.
25. Dadlez, M. & Kim, P. (1995). Detection of a third native one-disulfide intermediate in the folding of BPTI. Nature Struct. Biol. 2, 6-12.
26. Wüthrich, K. (1994). NMR assignments as a basis for structural characterization of denatured states of globular proteins. Curr. Opin. Struct. Biol. 4, 93-99.
27. Sandström, J. (1982). Dynamic NMR. Academic Press, New York.
28. Shortle, D. (1995). Staphylococcal nuclease: a showcase of m-value effects [Review]. Adv. Protein Chem. 46, 217-247.
29. Tidor, B. & Karplus M. (1993). The contribution of crosslinks to protein stability: a normal mode analysis of the configurational entropy of the native state. Proteins 15, 71-79.
30. Betz, S. (1993). Disulfide bonds and the stability of globular proteins. Protein Sci. 2, 1551-1558.
31. Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. (1979). Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553 .
32. 1H spin system identification in macromolecules. J. Am. Chem. Soc. 110, 7870-7872.
33. Berndt, K.D., Güntert, P., Orbons, L.P.M. & Wüthrich, K. (1992). Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic inhibitor and comparison with three crystal structures. J. Mol. Biol. 227, 757-775.
34. Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
35. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallgr. 24, 946-950.