Protein side-chain conformation: A systematic variation of χ1 mean values with resolution - A consequence of multiple rotameric states?

Acta Crystallographica Section D: Biological Crystallography

Volumn 55, Issue 5, 1999, Pages 994-1004

  MacArthur, Malcolm W ^a   Thornton, Janet M ^a,b  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; CYSTEINE; PROTEIN; SOLVENT;

ARTICLE; CHEMISTRY; COMPARATIVE STUDY; METHODOLOGY; PROTEIN CONFORMATION; ROTATION; SOLUBILITY; X RAY CRYSTALLOGRAPHY;

ASPARAGINE; ASPARTIC ACID; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; PROTEIN CONFORMATION; PROTEINS; ROTATION; SOLUBILITY; SOLVENTS;

EID: 0033135979     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444999002231     Document Type: Article

References (26)

1. Akke, M., Liu, J., Cavanagh, J., Erickson, H. P. & Palmer, A. G. (1998). Nature Struct. Biol. 5, 55-59.
2. Batchelder, L. S., Sullivan, C. E., Jelinski, L. W. & Torchia, D. A. (1982). Proc. Natl Acad. Sci. USA, 79, 386-389.
3. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F. Jr, Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977). J. Mol. Biol. 122, 535-542.
4. Burling, F. T. & Brünger, A. T. (1994). Isr. J. Chem. 34, 165-175.
5. Carugo, O. & Argos, P. (1997). Protein Eng. 10, 777-787.
6. Colnago, L. A., Valentine, K. G. & Opella, S. J. (1987). Biochemistry, 26, 847-854.
7. Dahms, T. E. S., Willis, K. J. & Szabo, A. G. (1995). J. Am. Chem. Soc. 117, 2321-2326.
8. Dauter, Z., Lamzin, V. S. & Wilson, K. S. (1995). Curr. Opin. Struct. Biol. 5, 784-790.
9. Desmet, J., Wilson, I. A., Joniau, M., De Maeyer, M. & Lasters, I. (1997). FASEB J. 11, 164-172.
10. Dunbrack, R. L. & Karplus, M. (1993). J. Mol. Biol. 230, 543-574.
11. Frauenfelder, H., Parak, F. & Young, R. D. (1988). Annu. Rev. Biophys. Biophys. Chem. 17, 451-479.
12. Hooft, R. W. W., Sander, C. & Vriend, G. (1996). Proteins, 26, 363-376.
13. Hubbard, S. J. (1992). PhD thesis. University of London.
14. Hubbard, S. J., Campbell, S. F. & Thornton, J. M. (1991). J. Mol. Biol. 220, 507-530.
15. Lee, B. & Richards, F. M. (1971). J. Mol. Biol. 55, 379-400.
16. Lee, C. & Subbiah, S. (1991). J. Mol. Biol. 217, 373-388.
17. McDonald, I. K. & Thornton, J. M. (1995). Protein Eng. 8, 217-224.
18. Morris, A. L., MacArthur, M. W., Hutchinson, E. G. & Thornton, J. M (1992). Proteins, 12, 345-364.
19. Orengo, C. A. & Taylor, W. R. (1996). Methods Enzymol. 266, 617-634.
20. Picket, S. D. & Sternberg, M. J. E. (1993). J. Mol. Biol. 231, 825-839.
21. Rejto, P. A. & Freer, S. T. (1996). Prog. Biophys. Mol. Biol. 66, 167-196.
22. Smith, J. L., Hendrickson, W. A., Honzatko, R. B. & Sheriff, S. (1986). Biochemistry, 25, 5018-5027.
23. Stec, B., Zhou, R. S. &Teeter, M. M. (1995). Acta Cryst. D51, 663-681.
24. Swindells, M. B., MacArthur, M. W. & Thornton, J. M. (1995). Nature Struct. Biol. 2, 596-603.
25. Wüthrich, K. (1986). NMR of Proteins. New York: Wiley.
26. Yang, D. W., Mittermaier, A., Mok, Y. K. & Kay, L. E. (1998). J. Mol. Biol. 276, 939-954.