The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin

Biochemistry

Volumn 37, Issue 22, 1998, Pages 8071-8079

  Hamill, Stefan J ^a   Meekhof, Alison E ^a   Clarke, Jane ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; TENASCIN;

AMINO ACID SEQUENCE; ARTICLE; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ALANINE; CIRCULAR DICHROISM; FIBRONECTINS; HUMANS; HYDROGEN; KINETICS; LEUCINE; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TENASCIN; THERMODYNAMICS;

EID: 0032474435     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9801659     Document Type: Article

References (48)

1. Chothia, C. (1992) Nature 357, 543-544.
2. Gerstein, M., and Levitt, M. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 11911-11916.
3. Bork, P., and Doolittle, R. F. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 8990-8994.
4. Williams, A. F., and Barclay, A. N. (1988) Annu. Rev. Immunol. 6, 381-405.
5. Baron, M., Norman, D. G., and Campbell, I. D. (1991) Trends Biochem. Sci. 16, 13-17.
6. Patel, R. S., Odermatt, E., Schwarzbauer, J. E., and Hynes, R. O. (1987) EMBO J. 6, 2565-2572.
7. Cohen, S. L. (1996) Structure 4, 1013-1016.
8. Dickinson, C. D., Gay, D. A., Parello, J., Ruoslahti, E., and Ely, K. R. (1994) J. Mol. Biol. 238, 123-127.
9. Pfuhl, M., Improta, S., Politou, A. S., and Pastore, A. (1997) J. Mol. Biol. 265, 242-256.
10. Politou, A. S., Gautel, M., Joseph, C., and Pastore, A. (1994) FEBS Lett. 352, 27-31.
11. Clarke, J., Hamill, S. J., and Johnson, C. M. (1997) J. Mol. Biol. 270, 771-778.
12. Leahy, D. J., Hendrickson, W. A., Aukhil, I., and Erickson, H. P. (1992) Science 258, 987-991.
13. Glasoe, P. F., and Long, F. A. (1960) J. Phys. Chem. 64, 188-193.
14. Clarke, J., Hounslow, A. M., Bycroft, M., and Fersht, A. R. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 9837-9841.
15. Jackson, S. E., elMasry, N., and Fersht, A. R. (1993) Biochemistry 32, 11270-11278.
16. Itzhaki, L. S., Otzen, D. E., and Fersht, A. R. (1995) J. Mol. Biol. 254, 260-288.
17. Fersht, A. R., Matouschek, A., and Serrano, L. (1992) J. Mol. Biol. 224, 771-782.
18. Hvidt, A. A., and Nielsen, S. O. (1966) Adv. Protein Chem. 21, 287-386.
19. Roder, H., Wagner, G., and Wütrich, K. (1985) Biochemistry 24, 7396-7407.
20. Perrett, S., Clarke, J., Hounslow, A. M., and Fersht, A. R. (1995) Biochemistry 34, 9288-9298.
21. Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Science 269, 192-197.
22. Swint-Kruse, L., and Robertson, A. D. (1996) Biochemistry 35, 171-180.
23. Skelton, N. J., Kordel, J., Akke, M., and Chazin, W. J. (1992) J. Mol. Biol. 227, 1100-1117.
24. Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Proteins: Struct., Funct., Genet. 17, 75-86.
25. Nies, D. E., Hemesath, T. J., Kim, J. H., Gulcher, J. R., and Stefansson, K. (1991) J. Biol. Chem. 266, 2818-2823.
26. Serrano, L., Kellis, J., Cann, P., Matouschek, A., and Fersht, A. R. (1992) J. Mol. Biol. 224, 783-804.
27. Kim, K. S., Fuchs, J. A., and Woodward, C. K. (1993) Biochemistry 32, 9600-9608.
28. Pfuhl, M., and Pastore, A. (1995) Structure 3, 391-401.
29. Fong, S., Hamill, S. J., Procter, M., Freund, S. M. V., Benian, G. M., Chothia, C., Bycroft, M., and Clarke, J. (1996) J. Mol. Biol. 264, 624-639.
30. Leahy, D. J., Aukhil, I., and Erickson, H. P. (1996) Cell 84, 155-164.
31. Plaxco, K. W., Spitzfaden, C., Campbell, I. D., and Dobson, C. M. (1997) J. Mol. Biol. 270, 763-770.
32. Finkelstein, A. V. (1991) Proteins: Struct., Funct., Genet. 9, 23-27.
33. Jackson, S. E., and Fersht, A. R. (1991) Biochemistry 30, 10428-10435.
34. Chen, B.-L., Baase, W. A., Nicholson, H., and Schellman, J. A. (1992) Biochemistry 31, 1464-1476.
35. Tskhovrebova, L., Trinick, J., Sleep, J. A., and Simmons, R. M. (1997) Nature 387, 308-312.
36. Politou, A. S., Thomas, D. J., and Pastore, A. (1995) Biophys. J. 69, 2601-2610.
37. Soteriou, A., Clarke, A., Martin, S., and Trinick, J. (1993) Proc. R. Soc. London B. 254, 83-86.
38. Erickson, H. P. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10114-10118.
39. Rief, M., Gauiel, M., Oesterhelt, F., Fernandez, J. M., and Gaub, H. E. (1997) Science 276, 1109-1112.
40. Litvinovich, S. V., and Ingham, K. C. (1995) J. Mol. Biol. 245, 611-626.
41. Spitzfaden, C., Grant, R. P., Mardon, H. J., and Campbell, I. D. (1997) J. Mol. Biol. 265, 565-579.
42. Akke, M., Liu, J., Cavanagh, J., Erickson, H. P., and Palmer, A. G. (1998) Nat. Struct. Biol. 5, 55-59.
43. Plaxco, K. W., Spitzfaden, C., Campbell, I. D., and Dobson, C. M. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 10703-10706.
44. Carr, P. A., Erickson, H. P., and Palmer, A. G. (1997) Structure 5, 949-959.
45. Baron, M., Main, A. L., Driscoll, P. C., Mardon, H. J., Boyd, J., and Campbell, I. D. (1992) Biochemistry 31, 2068-2073.
46. Main A. L., Harvey, T. S., Baron, M., Boyd, J., and Campbell, I. D. (1992) Cell 71, 671-678.
47. Pace, C. N. (1986) Methods Enzymol. 131, 266-279.
48. Kraulis, P. (1991) J. Appl. Crystallogr. 24, 946-950.