Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation [5]

Journal of the American Chemical Society

Volumn 121, Issue 42, 1999, Pages 9879-9880

  Andersen, Niels H ^a   Dyer, R Brian ^b   Fesinmeyer, R Matthew ^a   Gai, Feng ^b   Liu, Zhihong ^a   Neidigh, Jonathan W ^a   Tong, Hui ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DERIVATIVE; CARBON 13; PEPTIDE;

CARBON NUCLEAR MAGNETIC RESONANCE; FOURIER TRANSFORMATION; HYDROPHOBICITY; INFRARED SPECTROMETRY; LETTER; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; THERMODYNAMICS;

EID: 0033610474     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja991829k     Document Type: Letter

References (15)

1. Becktel, W. J.; Schellman, J. A. Biopolymers 1987, 26, 1859-1877. Privalov, P. L. Crit. Rev. Biochem. Mol. Biol. 1990, 25, 281-305.
2. Becktel, W. J.; Schellman, J. A. Biopolymers 1987, 26, 1859-1877. Privalov, P. L. Crit. Rev. Biochem. Mol. Biol. 1990, 25, 281-305.
3. (a) Andersen, N. H.; Cort, J. R.; Liu, Z.; Sjoberg, S. J.; Tong, H. J. Am. Chem. Soc. 1996, 118, 10309-10310.
4. (b) Lacassie, E.; Delmas, A.; Meunier, C.; Sy, D.; Trudelle, Y. Int. J. Pept. Protein Res. 1996, 48, 249-258.
5. All concentrations of cosolvents are given in volume percent.
6. (a) de Alba, E.; Jiménez, M. A.; Rico, M.; Nieto, J. Folding Des 1996, 1, 133-144.
7. (b) Ramírez-Alvarado, M.; Blanco, F. J.; Niemann, H.; Serrano, L. J. Mol. Biol. 1997, 273, 898-912.
8. (c) Sharman, G. J.; Searle, M. S. Chem. Commun. 1997, 1955-1956.
9. Maynard, A. J.; Sharman, G. J.; Searle, M. S. J. Am. Chem. Soc. 1998, 120, 1996-2007.
10. Andersen, N. H.; Liu, Z.; Prickett, K. S. FEBS Lett. 1996, 399, 47-52.
11. Wishart, D. S.; Sykes, B. D. Methods Enzymol. 1994, 239, 363-392.
12. Andersen, N. H.; Neidigh, J. W.; Harris, S. M.; Lee, G. M.; Liu, Z.; Tong, H. J. Am. Chem. Soc. 1997, 119, 8547-8561.
13. Chakrabartty, A.; Kortemme, T.; Baldwin, R. L. Protein Sci. 1994, 3, 843-852.
14. The instrumentation and methods used for the FT-IR studies have been published previously: Williams, S.; Causgrove, T. P.; Gilmanshin, R.; Fang, K. S.; Callender, R. H.; Woodruff, W. H.; Dyer, R. B. Biochemistry 1996, 35, 691-697.
15. 13C NMR studies also reveal distinct behavior for the two centrally labeled sites of YGG-3V. All four helix bands of YGG-3V increase with temperature over the range from 3 to 25 °C, indicating a cooperative cold denaturation transition that includes both the solvated and solvent-protected helical sites. At temperatures higher than 25 °C, YGG-3V becomes less helical upon further warming.