A molecular mechanism for osmolyte-induced protein stability

作者: T. O. Street , D. W. Bolen , G. D. Rose

DOI: 10.1073/PNAS.0606236103

关键词:

摘要: … molecular theory that can explain the mechanism by which osmolytes interact with the protein … mechanics backbone solvation model in which the interaction energy depends on interac- …

参考文章(38)
W. L. Delano, The PyMOL Molecular Graphics System DeLano Scientific. ,(2002)
Yasuhiko Nozaki, Charles Tanford, THE SOLUBILITY OF AMINO ACIDS AND RELATED COMPOUNDS IN AQUEOUS UREA SOLUTIONS. Journal of Biological Chemistry. ,vol. 238, pp. 4074- 4081 ,(1963) , 10.1016/S0021-9258(18)51830-5
J.C. Lee, S.N. Timasheff, The stabilization of proteins by sucrose. Journal of Biological Chemistry. ,vol. 256, pp. 7193- 7201 ,(1981) , 10.1016/S0021-9258(19)68947-7
George I. Makhatadze, Peter L. Privalov, Protein interactions with urea and guanidinium chloride. A calorimetric study. Journal of Molecular Biology. ,vol. 226, pp. 491- 505 ,(1992) , 10.1016/0022-2836(92)90963-K
Raymond F. Greene, C. Nick Pace, Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and b-Lactoglobulin Journal of Biological Chemistry. ,vol. 249, pp. 5388- 5393 ,(1974) , 10.1016/S0021-9258(20)79739-5
Daniel J. Felitsky, Jonathan G. Cannon, Michael W. Capp, Jiang Hong, Adam W. Van Wynsberghe, Charles F. Anderson, M. Thomas Record, The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry. ,vol. 43, pp. 14732- 14743 ,(2004) , 10.1021/BI049115W
Joseph D. Batchelor, Alina Olteanu, Ashutosh Tripathy, Gary J. Pielak, Impact of protein denaturants and stabilizers on water structure. Journal of the American Chemical Society. ,vol. 126, pp. 1958- 1961 ,(2004) , 10.1021/JA039335H
R. S. Spolar, J. H. Ha, M. T. Record, Hydrophobic effect in protein folding and other noncovalent processes involving proteins Proceedings of the National Academy of Sciences of the United States of America. ,vol. 86, pp. 8382- 8385 ,(1989) , 10.1073/PNAS.86.21.8382