Direct observation of tug-of-war during the folding of a mutually exclusive protein

Journal of the American Chemical Society

Volumn 131, Issue 37, 2009, Pages 13347-13354

  Peng, Qing ^a   Li, Hongbin ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX DYNAMICS; CONFORMATIONAL EQUILIBRIUM; DIRECT OBSERVATION; FOLDED STRUCTURES; FOLDING DYNAMICS; FOLDING KINETICS; HOST PROTEINS; KINETIC COUPLING; KINETIC EVIDENCE; MECHANICAL STRAIN; MODEL SYSTEM; MULTIDOMAIN PROTEINS; PROTEOMES; SINGLE-DOMAIN PROTEINS; SINGLE-MOLECULE; STOPPED-FLOW TECHNIQUES; SURFACE LOOPS; THREE-DIMENSIONAL STRUCTURE; TOPOLOGICAL CONSTRAINTS; TWO DOMAINS;

ATOMIC FORCE MICROSCOPY; CONFORMATIONS; MILITARY OPERATIONS; THERMODYNAMIC STABILITY; THERMODYNAMICS;

PROTEIN FOLDING;

PROTEOME;

ARTICLE; ATOMIC FORCE MICROSCOPY; KINETICS; MOLECULAR BIOLOGY; MOLECULAR DYNAMICS; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEOMICS; THERMODYNAMICS;

AMINO ACID SEQUENCE; BIOMECHANICS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; THERMODYNAMICS;

EID: 70349386569     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja903480j     Document Type: Article

References (29)

1. Ponting, C. P.; Russell, R. R. Annu. Rev. Biophys. Biomol. Struct. 2002, 31, 45-71.
2. Vogel, C.; Berzuini, C.; Bashton, M.; Gough, J.; Teichmann, S. A. J. Mol. Biol. 2004, 336, 809-823.
3. Selvam, R. A.; Sasidharan, R. Nucleic Acids Res. 2004, 32 (Database issue), D193-D195.
4. Aroul-Selvam, R.; Hubbard, T.; Sasidharan, R. J. Mol. Biol. 2004, 338, 633-641.
5. Radley, T. L.; Markowska, A. I.; Bettinger, B. T.; Ha, J. H.; Loh, S. N. J. Mol. Biol. 2003, 332, 529-536.
6. Cutler, T. A.; Loh, S. N. J. Mol. Biol. 2007, 371, 308-316.
7. Cutler, T. A.; Mills, B. M.; Lubin, D. J.; Chong, L. T.; Loh, S. N. J. Mol. Biol. 2009, 386, 854-868.
8. Li, H.; Wang, H. C.; Cao, Y.; Sharma, D.; Wang, M. J. Mol. Biol. 2008, 379, 871-880.
9. Carrion-Vazquez, M.; Oberhauser, A. F.; Fowler, S. B.; Marszalek, P. E.; Broedel, S. E.; Clarke, J.; Fernandez, J. M. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 3694-3699.
10. Rief, M.; Gautel, M.; Oesterhelt, F.; Fernandez, J. M.; Gaub, H. E. Science 1997, 276, 1109-1112.
11. Cao, Y.; Li, H. Nat. Mater. 2007, 6, 109-114.
12. Improta, S.; Politou, A. S.; Pastore, A. Structure 1996, 4, 323-337.
13. McCallister, E. L.; Alm, E.; Baker, D. Nat. Struct. Biol. 2000, 7, 669-673.
14. Gronenborn, A. M.; Filpula, D. R.; Essig, N. Z.; Achari, A.; Whitlow, M.; Wingfield, P. T.; Clore, G. M. Science 1991, 253, 657-661.
15. Gallagher, T.; Alexander, P.; Bryan, P.; Gilliland, G. L. Biochemistry 1994, 33, 4721-4729.
16. Politou, A. S.; Thomas, D. J.; Pastore, A. Biophys. J. 1995, 69, 2601-2610.
17. Vuilleumier, S.; Sancho, J.; Loewenthal, R.; Fersht, A. R. Biochemistry 1993, 32, 10303-10313.
18. Gur, E.; Sauer, R. T. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 16113-16118.
19. Clarke, J.; Hamill, S. J.; Johnson, C. M. J. Mol. Biol. 1997, 270, 771-778.
20. Although unlikely, the reason that the fluorescence does not return to the initial value could be that the GL5 domain (in the vicinity of the tryptophan) remains partially folded. Our current data cannot completely rule out this possibility.
21. Cao, Y.; Li, H. J. Mol. Biol. 2008, 375, 316-324.
22. Viguera, A. R.; Serrano, L. Nat. Struct. Biol. 1997, 4, 939-946.
23. Grantcharova, V. P.; Riddle, D. S.; Baker, D. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 7084-7089.
24. Scalley-Kim, M.; Minard, P.; Baker, D. Protein Sci. 2003, 12, 197-206.
25. Fersht, A. R. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 1525-1529.
26. Nagi, A. D.; Anderson, K. S.; Regan, L. J. Mol. Biol. 1999, 286, 257-265.
27. Peng, Q.; Li, H. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 1885-1890.
28. Sharma, D.; Perisic, O.; Peng, Q.; Cao, Y.; Lam, C.; Lu, H.; Li, H. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 9278-9283.
29. Fernandez, J. M.; Li, H. Science 2004, 303, 1674-1678.