Cold denaturation of monomeric peptide helices

Journal of the American Chemical Society

Volumn 118, Issue 42, 1996, Pages 10309-10310

  Andersen, Niels H ^a   Cort, John R ^a   Liu, Zhinhong ^a   Sjoberg, Sandra J ^a   Tong, Hui ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CIRCULAR DICHROISM; PROTEIN DENATURATION; TEMPERATURE;

EID: 0029990821     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961143h     Document Type: Article

References (36)

1. (a) Becktel, W. J.; Schellman, J. A. Biopolymers 1987, 26, 1859-1877.
2. (b) Privalov, P. L. Crit. Rev. Biochem. Mol. Biol 1990, 25, 281-305.
3. Pace, N. C.; Tanford, C. Biochemistry 1968, 7, 198-208.
4. Privalov, P. L.; Griko, Y. V.; Venyaminov, S. Y.; Kutyshenko, V. P. J. Mol. Biol. 1986, 190, 487-498.
5. (a) Nishii, I.; Kataoka, M.; Tokunaga, F.; Goto, Y. Biochemistry 1994, 33, 4903-4909.
6. (b) Carra, J. H.; Anderson, E. A.; Privalov, P. L. Protein Sci. 1994, 3, 952-959.
7. (c) Kuroda, Y.; Kidokoro, S.; Wada, A. J. Mol. Biol. 1992, 223, 1139-1153.
8. (a) Kitakuni, E.; Kuroda, Y.; Oobatake, M.; Tanaka, T.; Nakamura, H. Protein Sci. 1994, 3, 831-837.
9. (b) Hagihara, Y.; Oobatake, M.; Goto, Y. Protein Sci. 1994, 3, 1418-1429.
10. 8 (b) A partially folded icosamer has been reported to display a broader distribution of endto-end distances on cooling (Beals, J. M.; Haas, E.; Krausz, S.; Scheraga, H. A. Biochemistry 1991, 30, 7680-7692).
11. 8 (b) A partially folded icosamer has been reported to display a broader distribution of endto-end distances on cooling (Beals, J. M.; Haas, E.; Krausz, S.; Scheraga, H. A. Biochemistry 1991, 30, 7680-7692).
12. -1)res (Shalongo, W.; Dugad, L.; Stellwagen, E. J. Am. Chem. Soc. 1994, 116, 2500-2507).
13. Forood, B.; Feliciano, E. J.; Nambiar, K. P. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 838-842.
14. Woody, R. W. Adv. Biophys. Chem. 1992, 2, 37-79.
15. For example see: Scholtz, J. M.; Marqusee, S.; Baldwin, R. L.; York, E. J.; Stewart, J. M.; Santoro, M.; Bolen, D. W. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 2854-2858.
16. (a) Murphy, K. P.; Freire, E. Adv. Protein Chem. 1992, 43, 313-361.
17. (b) Ooi, T.; Oobatake, M. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 2859-2863.
18. Griko, Y. V.; Privalov, P. L.; Sturtevant, J. M.; Venyaminov, S. Y. Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 3343-3347.
19. 6a,8
20. The thermal dependence of [θ] for YGG-3V and -3T and sCT(8-32) in aqueous HFIP is concentration independent (5-90 μM). For other peptides, concentration independent cold denaturation has been observed over a much larger range of concentration (5 μM to 1.6 mM).
21. (a) Nelson, J. W.; Kallenbach, N. R. Proteins: Struct., Funct., Genet. 1986, 1, 211-217.
22. (b) Merutka, G.; Stellwagen, E. Biochemistry 1989, 28, 352-357.
23. (c) Shoemaker, K. R.; Fairman, R.; Schultz, D. A.; Robertson, A. D.; York, E. J.; Stewart, J. M.; Baldwin, R. L. Biopolymers 1990, 29, 1-11.
24. (d) Jasanoff, A.; Fersht, A. R. Biochemistry 1994, 33, 2129-2135.
25. (e) Blanco, F. J.; Jiménez, M. A.; Pineda, A.; Rico, M.; Santoro, J.; Nieto, J. L. Biochemistry 1994, 33, 6004-6014.
26. (f) Cammers-Goodwin, A.; Allen, T. J.; Oslick, S. L.; McClure, K. F.; Lee, J. H.; Kemp, D. S. J. Am. Chem. Soc. 1996, 118, 3083-3090 and references cited therein.
27. TFE partially denatures proteins by increasing helicity and reducing the hydrophobic interactions that result in tertiary and quarternary structure: (a) Buck, M.; Radford, S. E.; Dobson, C. M. Biochemistry 1993, 32, 669-678.
28. (b) Slupsky, C. M.; Kay, C. M.; Reinach, F. C.; Smillie, L. B.; Sykes, B. D. Biochemistry 1995, 34, 7365-7375.
29. Lifson, R.; Roig, A. J. Chem. Phys. 1961, 34, 1963-1974.
30. In the peptides studied, there are residues at both ends of the sequence which remain "random coil" in the folded state. These should not contribute to the thermodynamic parameters for unfolding. The residues that are helical in the folded state are shown on the peptide sequences.
31. 10a have established that the experimental convergence temperatures for AS and AH can differ, and there is no basis for assuming that a similar temperature would apply to aqueous HFIP medium.
32. 10a have established that the experimental convergence temperatures for AS and AH can differ, and there is no basis for assuming that a similar temperature would apply to aqueous HFIP medium.
33. 10a have established that the experimental convergence temperatures for AS and AH can differ, and there is no basis for assuming that a similar temperature would apply to aqueous HFIP medium.
34. -1)/res.
35. Our search of physicochemical studies of alcohol/water mixtures has located only one measure by which HFIP is distinguished from both TFE and iPrOH: HFIP/water mixtures display a large negative excess molar enthalpy of mixing at all mole fractions (Denda, M.; Touhara, H.; Nakanishi, K. J. Chem. Thermodyn. 1987, 19, 539-542).
36. Scholtz, J. M.; Barrick, D.; York, E. J.; Stewart, J. M.; Baldwin, R. L. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 185-189.