Φ-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 40, 2007, Pages 15717-15722

  Neudecker, Philipp ^a   Zarrine Afsar, Arash ^a   Davidson, Alan R ^a   Kay, Lewis E ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Carr Purcell Meiboom Gill; Chemical exchange; Fyn SH3; Protein folding intermediate; Transition state

Indexed keywords

ARTICLE; CONFORMATION; DISPERSION; GENE MUTATION; GENETIC ANALYSIS; KINETICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS;

AMINO ACID SUBSTITUTION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTATION; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTO-ONCOGENE PROTEINS C-FYN; RECOMBINANT PROTEINS; SRC HOMOLOGY DOMAINS;

EID: 35648945863     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0705097104     Document Type: Article

References (36)

1. Fersht A (1999) Structure and Mechanism in Protein Science (Freeman, New York).
2. Brockwell DJ, Radford SE (2007) Curr Opin Struct Biol 17:30-37.
3. Palmer AG (2004) Chem Rev 104:3623-3640.
4. Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE (2004) Nature 430:586-590.
5. Korzhnev DM, Neudecker P, Mittermaier A, Orekhov VY, Kay LE (2005) J Am Chem Soc 127:15602-15611.
6. Korzhnev DM, Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE (2006) Biochemistry 45:10175-10183.
7. Neudecker P, Zarrine-Afsar A, Choy W-Y, Muhandiram DR, Davidson AR, Kay LE (2006) J Mol Biol 363:958-976.
8. Matthews CR (1987) Methods Enzymol 154:498-511.
9. Goldenberg DP, Frieden RW, Haack JA, Morrison TB (1989) Nature 338:127-132.
10. Fersht AR, Matouschek A, Serrano L (1992) J Mol Biol 224:771-782.
11. Fersht A, Sato S (2004) Proc Natl Acad Sci USA 101:7976-7981.
12. Capaldi AP, Kleanthous C, Radford SE (2002) Nat Struct Biol 9:209-216.
13. Matouschek A, Serrano L, Fersht AR (1992) J Mol Biol 224:819-835.
14. Khan F, Chuang JI, Gianni S, Fersht AR (2003) J Mol Biol 333:169-186.
15. Nölting B, Golbik R, Fersht AR (1995) Proc Natl Acad Sci USA 92:10668-10672.
16. Nölting B, Golbik R, Neira JL, Soler-Gonzalez AS, Schreiber G, Fersht AR (1997) Proc Natl Acad Sci USA 94:826-830.
17. Neudecker P, Korzhnev DM, Kay LE (2006) J Biomol NMR 34:129-135.
18. Eyring H (1935) Chem Rev 17:65-77.
19. Cho J-H, Raleigh DP (2006) J Am Chem Soc 128:16492-16493.
20. Northey JGB, Di Nardo AA, Davidson AR (2002) Nat Struct Biol 9:126-130.
21. Zarrine-Afsar A, Dahesh S, Davidson AR (August 9, 2007) J Mol Biol, 10.1016/j.jmb.2007.07.059.
22. Martinez JC, Serrano L (1999) Nat Struct Biol 6:1010-1016.
23. Riddle DS, Grantcharova VP, Santiago JV, Alm E, Ruczinski I, Baker D (1999) Nat Struct Biol 6:1016-1024.
24. Noble MEM, Musacchio A, Saraste M, Courtneidge SA, Wierenga RK (1993) EMBO J 12:2617-2624.
25. Sosnick TR, Krantz BA, Dothager RS, Baxa M (2006) Chem Rev 106:1862-1876.
26. Guo W, Lampoudi S, Shea J-E (2003) Biophys J 85:61-69.
27. Wishart DS, Bigam CG, Holm A, Hodges RS, Sykes BD (1995) J Biomol NMR 5:67-81.
28. Wüthrich K (1986) NMR of Proteins and Nucleic Acids (Wiley, New York).
29. Wishart DS, Case DA (2001) Methods Enzymol 338:3-34.
30. Wishart DS, Sykes BD, Richards FM (1991) J Mol Biol 222:311-333.
31. Grey MJ, Tang Y, Alexov E, McKnight CJ, Raleigh DP, Palmer AG (2006) J Mol Biol 355:1078-1094.
32. Zhang O, Kay LE, Olivier JP, Forman-Kay JD (1994) J Biomol NMR 4:845-858.
33. Loria JP, Rance M, Palmer AG (1999) J Am Chem Soc 121:2331-2332.
34. Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE (2001) J Am Chem Soc 123:11341-11352.
35. Press WH, Teukolsky SA, Vetterling WT, Flannery BP (1992) Numerical Recipes in C (Cambridge Univ Press, Cambridge, UK), 2nd Ed.
36. Skrynnikov NR, Dahlquist FW, Kay LE (2002) J Am Chem Soc 124:12352-12360.