Site-specific NMR monitoring of cis-trans isomerization in the folding of the proline-rich collagen triple helix

Biochemistry

Volumn 39, Issue 15, 2000, Pages 4299-4308

  Buevich, Alexei V ^a   Dai, Qing Hong ^a   Liu, Xiaoyan ^a,b   Brodsky, Barbara ^c   Baum, Jean ^a  

^a RUTGERS UNIVERSITY   (United States)

^b Oral Care Research and Development   (United States)

^c RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COLLAGEN; NITROGEN 15; PROLINE; PROTON;

ARTICLE; GENE MUTATION; ISOMERISM; KINETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FOLDING; STATISTICAL ANALYSIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; BIOPOLYMERS; COLLAGEN; GLYCINE; HUMANS; ISOMERISM; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROLINE; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE; THERMODYNAMICS;

EID: 0034681942     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992584r     Document Type: Article

References (52)

1. Dyson, H. J., and Wright, P. E. (1998) Nat. Struct. Biol. 5 (Suppl.), 499-503.
2. Dobson, C. M., and Hore, P. J. (1998) Nat. Struct. Biol. 5 (Suppl.), 504-507.
3. Dill, K. A., and Chan, H. S. (1997) Nat. Struct. Biol. 4, 10-19.
4. Onuchic, J. N. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 7129-7131.
5. Rich, A., and Crick, F. H. C. (1961) J. Mol. Biol. 3, 483-506.
6. Nemethy, G., and Scheraga, H. A. (1982) Biopolymers 28, 1573-1584.
7. Bella, J., Eaton, M., Brodsky, B., and Berman, H. M. (1994) Science 266, 75-81.
8. Bella, J., Brodsky, B., and Berman, H. M. (1995) Structure 3, 893-906.
9. Brodsky, B. (1990) Folding and higher order structure in fibrous proteins, AAAS, Washington.
10. Kielty, C. M., Hopkinson, I., and Grant, M. E. (1993) The Collagen Family: Structure, Assembly, and Organization in the Extracellular Matrix, Wiley Liss, New York.
11. McLaughlin, S. H., and Bulleid, N. J. (1997) Matrix Biol. 16, 369-377.
12. Bächinger, H. P., Bruckner, P., Timpl, R., Prockop, D. J., and Engel, J. (1980) Eur. J. Biochem. 106, 619-632.
13. Bächinger, H. P., Bruckner, P., Timpl, R., and Engel, J. (1978) Eur. J. Biochem. 90, 605-613.
14. Harrison, R. K., and Stein, R. L. (1990) Biochemistry 29, 3813-3816.
15. Kuivaniemi, H., Tromp, G., and Prockop, D. (1997) Hum. Mutat. 9, 300-315.
16. Prockop, D. J., and Kivirikko, K. I. (1995) Annu. Rev. Biochem. 64, 403-434.
17. Byers, P. H. (1993) in Connective Tissue and Its Heritable Disorders: Molecular, Genetic, and Medical Aspects (Royce, P. M., and Steinmann, B., Eds.) pp 317-350, 351-407, Wiley Liss, New York.
18. Bächinger, H. P., Morris, N. P., and Davis, J. M. (1993) Am. J. Med. Gen. 45, 152-162.
19. Raghunath, M., Bruckner, P., and Steinmann, B. (1994) J. Mol. Biol. 236, 940-949.
20. Goodman, M., Feng, Y., Melacini, G., and Taulane, J. P. (1996) J. Am. Chem. Soc. 118, 5156-5157.
21. Mayo, K. H. (1996) Biopolymers 40, 359-370.
22. Feng, Y., Melacini, G., Taulane, J. P., and Goodman, M. (1996) J. Am. Chem. Soc. 118, 10351-10358.
23. Fields, G. B., and Prockop, D. J. (1996) Biopolymers 40, 345-357.
24. Baum, J., and Brodsky, B. (1999) Curr. Opin. Struct. Biol. 9, 122-128.
25. Baum, J., and Brodsky, B. (1999) in Protein Folding: Frontiers in Molecular Biology (Pain, R. H., Ed.) Oxford University Press (in press).
26. Baum, J., and Brodsky, B. (1997) Folding Des. 2, R53-R60.
27. Liu, X., Siegel, D. L., Fan, P., Brodsky, B., and Baum, J. (1996) Biochemistry 35, 4306-4313.
28. Kay, L. E., Keifer, P., and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665.
29. Fesik, S. W., and Zuiderweg, E. R. P. (1988) J. Magn. Reson. 78, 588-593.
30. Farrow, N. A., Muhandiran, R., Singer, A., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., and Kay, L. E. (1994) Biochemistry 33, 5984-6003.
31. Cavanagh, J., Fairbrother, W. J., Palmer, A. G., III, and Skelton, N. J. (1996) Protein NMR Spectroscopy: Principles and Practice, Academic Press, Inc, New York.
32. Shampine, L. F., and Gordon, M. K. (1975) Computer Solutions of Ordinary Differential Equaiotns: The Initial Value Problem, W. H. Freeman, San Francisco.
33. Bevington, P. R., and Robinson, D. K. (1992) Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, New York.
34. Farrow, N. A., Zhang, O., Forman-Kay, J. D., and Kay, L. E. (1994) J. Biomol. NMR 4, 727-734.
35. Yang, W., Battinenni, M., and Brodsky, B. (1997) Biochemistry 36, 6930-6935.
36. Liu, X., Kim, S., Dai, Q.-H., Brodsky, B., and Baum, J. (1998) Biochemistry 33, 15528-15533.
37. Günther, H. (1995) NMR spectroscopy. John Wiley & Sons, New York.
38. Grathwohl, C., and Wüthrich, K. (1976) Biopolymers 15, 2025-2041.
39. Grathwohl, C., and Wüthrich, K. (1981) Biopolymers 20, 2623-2633.
40. Schmid, F. X. (1993) Annu. Rev. Biophys. Biomol. Struct. 22, 123-143.
41. Reimer, U., Scherer, G., Drewello, M., Kruber, S., Schutkowski, M., and Fischer, G. (1998) J. Mol. Biol. 279, 449-460.
42. Mayo, K. H., Parra-Diaz, D., McCarthy, J. B., and Chelberg, M. (1991) Biochemistry 30, 8251-8267.
43. Fischer, H., and Schmid F. X. (1990) Biochemistry 29, 2205-2212.
44. Sarkar, S. K., Young, P. E., Sullivan, C. E., and Torchia, D. A. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 4800-4803.
45. Bulleid, N. J., Wilson, R., and Lees, J. F. (1996) Biochem. J. 317, 195-202.
46. Bansal, M., and Ananthanarayanan, V. S. (1988) Biopolymers 27, 299-312.
47. Brant, D. A., Miller, W. G., and Flory, P. J. (1967) J. Mol. Biol. 23, 47-65.
48. Schimmel, P. R., and Flory, P. J. (1968) J. Mol. Biol. 34, 105-120.
49. Harrington, W., and von Hippel, P. H. (1961) Arch. Biochem. Biophys. 92, 110.
50. Balbach, J., Forge, V., vanNuland, N. A. J., Winder, S. L., Hore, P. J., and Dobson, C. M. (1995) Nat. Struct. Biol. 2, 865-870.
51. Balbach, J., Steegborn, C., Schindler, T., and Schmid, F. X. (1999) J. Mol. Biol. 285, 829-842.
52. Bächinger, H. P. (1987) J. Biol. Chem. 262, 17144-17148.