Compaction during protein folding studied by real-time NMR diffusion experiments [6]

Journal of the American Chemical Society

Volumn 122, Issue 24, 2000, Pages 5887-5888

  Balbach, Jochen ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE;

DIFFUSION; HYDRODYNAMICS; LETTER; LIGHT SCATTERING; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EID: 0034697642     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja994514d     Document Type: Letter

References (28)

1. Arai, M.; Ikura, T.; Semisotnov, G. V.; Kihara, H.; Amemiya, Y.; Kuwajima, K. J. Mol. Biol. 1998, 275, 149-162.
2. Eliezer, D.; Jennings, P. A.; Wright, P. E.; Doniach, S.; Hodgson, K. O.; Tsuruta, H. Science 1995, 270, 487-488.
3. Semisotnov, G. V.; Kihara, H.; Kotova, N. V.; Kimura, K.; Amemiya, Y.; Wakabayashi, K.; Serdyuk, I. N.; Timchenko, A. A.; Chiba, K.; Nikaido, K.; Ikura, T.; Kuwajima, K. J. Mol. Biol. 1996, 262, 559-574.
4. Segel, D. J.; Bachmann, A.; Hofrichter, J.; Hodgson, K. O.; Doniach, S.; Kiefhaber, T. J. Mol. Biol. 1999, 288, 489-499.
5. Nöppert, A.; Gast, K.; Zirwer, D.; Damaschun, G. Folding Des. 1998, 3, 213-221.
6. Dobson, C. M.; Sali, A.; Karplus, M. Angew. Chem., Int. Ed. Engl. 1998, 37, 868-893.
7. Kuwajima, K. Proteins: Struct., Funct., Genet. 1989, 6, 87-103.
8. Schulman, B. A.; Kim, P. S.; Dobson, C. M.; Redfield, C. Nat. Struct. Biol. 1997, 4, 630-634.
9. Dolgikh, D. A.; Abaturov, L. V.; Bolotina, I. A.; Brazhnikov, E. V.; Bychkova, V. E.; Gilmanshin, R. I.; YuO, L.; Semisotnov, G. V.; Tiktopulo, E. I.; Ptitsyn, O. B. Eur. Biophys. J. 1985, 13, 109-121.
10. Flanagan, J. M.; Kataoka, M.; Fujisawa, T.; Engelman, D. M. Biochemistry 1993, 32, 10359-10370.
11. Kataoka, M.; Nishii, I.; Fujisawa, T.; Ueki, T.; Tokunaga, F.; Goto, Y. J. Mol. Biol. 1995, 249, 215-228.
12. Kataoka, M.; Kuwajima, K.; Tokunaga, F.; Goto, Y. Protein Sci. 1997, 6, 422-430.
13. Gast, K.; Damaschun, H.; Misselwitz, R.; Müller-Frohne, M.; Zirwer, D.; Damaschun, G. Eur. Biophys. J. 1994, 23, 297-305.
14. Wilkins, D. K.; Grimshaw, S. B.; Receveur, V.; Dobson, C. M.; Jones, J. A.; Smith, L. J. Biochemistry 1999, 38, 16424-16431.
15. Jones, J. A.; Wilkins, D. K.; Smith, L. J.; Dobson, C. M. J. Biomol. NMR 1997, 10, 199-203.
16. 15
17. Gast, K.; Zirwer, D.; Müller-Frohne, M.; Damaschun, G. Protein Sci. 1998, 7, 2004-2011.
18. Denisov, V. P.; Jonsson, B. H.; Halle, B. Nat. Struct. Biol. 1999, 6, 253-260.
19. Wilkins, D. K.; Ph.D. Thesis, University of Oxford, 1998.
20. 14
21. Balbach, J.; Forge, V.; van Nuland, N. A. J.; Winder, S. L.; Hore, P. J.; Dobson, C. M. Nat. Struct. Biol. 1995, 2, 865-870.
22. van Nuland, N. A. J., Forge, V.; Balbach, J.; Dobson, C. M. Acc. Chem. Res. 1998, 31, 773-780.
23. 4
24. Forge, V.; Wijesingha, R. T.; Balbach, J.; Brew, K.; Robinson, C. V.; Redfield, C.; Dobson, C. M. J. Mol. Biol. 1999, 288, 673-688.
25. 15 has been used at 600 MHz, 5°C, with a 30 ms diffusion time. Each curve is an average of three separate experiments with typically 64 scans per gradient strength and a sweep width of 9615 Hz. The NMR intensity of the protein (0.49 mM) was obtained by integrating the spectrum between 0.65 and 0.75 ppm.
26. A series of 42 PFG-SLED experiments such as in Figure 1 were performed during 5000 s with eight scans for each of the 10 different gradient strengths (10-100%, step 10%) per experiment. The first four sets up to 480 s and four sets between 2290 and 2770 s are presented.
27. Stejskal, E. O.; Tanner, J. E. J. Chem. Phys. 1965, 42, 288-292.
28. Gibbs, S. J.; Johnson, C. S., Jr. J. Magn. Reson. 1991, 93, 395-402.