Different effects of zwitterion and ethylene glycol on proteins

Journal of Chemical Physics

Volumn 136, Issue 22, 2012, Pages

  Shao, Qing ^a   He, Yi ^a   White, Andrew D ^a   Jiang, Shaoyi ^a  

^a University of Washington   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPHILICS; AVERAGE NUMBERS; BULK WATER; CARBOXYBETAINE; CHYMOTRYPSIN INHIBITOR 2; COMMON PROPERTY; DIFFERENT EFFECTS; HYDROPHOBIC DOMAINS; HYDROPHOBIC INTERACTIONS; MINIMAL EFFECTS; MODEL PROTEINS; MOLECULAR DYNAMICS SIMULATIONS; RADIAL DISTRIBUTION FUNCTIONS; ROOT MEAN SQUARE DEVIATIONS; SUPER-HYDROPHILIC; SURFACE AREA;

ETHYLENE GLYCOL; HYDROGEN BONDS; HYDROPHOBICITY; MOLECULAR DYNAMICS;

PROTEINS;

CHYMOTRYPSIN INHIBITOR 2; ETHYLENE GLYCOL; PEPTIDE; PROTEIN; VEGETABLE PROTEIN;

ARTICLE; CHEMISTRY; DRUG EFFECT; MOLECULAR DYNAMICS;

ETHYLENE GLYCOL; MOLECULAR DYNAMICS SIMULATION; PEPTIDES; PLANT PROTEINS; PROTEINS;

EID: 84866893168     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.4726135     Document Type: Article

References (42)

1. T. Serge N, in Advances in Protein Chemistry, edited by, D. S. E. Frederic, M. Richards, and, S. K. Peter, (Academic, 1998), p. 355.
2. S. N. Timasheff, Proc. Natl. Acad. Sci. U.S.A. 99, 9721 (2002). 10.1073/pnas.122225399
3. P. H. Yancey, J. Exp. Biol. 208, 2819 (2005). 10.1242/jeb.01730
4. H. J. Wiggers, J. Cheleski, A. Zottis, G. Oliva, A. D. Andricopulo, and C. A. Montanari, Anal. Biochem. 370, 107 (2007). 10.1016/j.ab.2007.06.042
5. B. N. Gangadhara, P. R. Kumar, and V. Prakash, J. Am. Oil Chem. Soc. 86, 773 (2009). 10.1007/s11746-009-1408-1
6. P. Attri, P. Venkatesu, and M. J. Lee, J. Phys. Chem. B 114, 1471 (2010). 10.1021/jp9092332
7. L. X. Chen, Y. Q. Gao, and D. H. Russell, J. Phys. Chem. A 116, 689 (2012). 10.1021/jp209430q
8. D. Shukla, C. P. Schneider, and B. L. Trout, J Am. Chem. Soc. 133, 18713 (2011). 10.1021/ja205215t
9. J. R. Livingstone, R. S. Spolar, and M. T. Record, Biochemistry 30, 4237 (1991). 10.1021/bi00231a019
10. M. W. Capp, L. M. Pegram, R. M. Saecker, M. Kratz, D. Riccardi, T. Wendorff, J. G. Cannon, and M. T. Record, Biochemistry 48, 10372 (2009). 10.1021/bi901273r
11. B. M. Baynes and B. L. Trout, Biophys. J 87, 1631 (2004). 10.1529/biophysj.104.042473
12. B. J. Bennion and V. Daggett, Proc. Natl. Acad. Sci. U.S.A. 101, 6433 (2004). 10.1073/pnas.0308633101
13. V. Vagenende, M. G. S. Yap, and B. L. Trout, Biochemistry 48, 11084 (2009). 10.1021/bi900649t
14. L. Ma, L. Pegram, M. T. Record, and Q. Cui, Biochemistry 49, 1954 (2010). 10.1021/bi9020082
15. F. F. Liu, L. Ji, L. Zhang, X. Y. Dong, and Y. Sun, J Chem. Phys. 132, 225103 (2010). 10.1063/1.3453713
16. D. Shukla, C. P. Schneider, and B. L. Trout, Adv. Drug Delivery Rev. 63, 1074 (2011). 10.1016/j.addr.2011.06.014
17. H. Y. Wei, Y. B. Fan, and Y. Q. Gao, J. Phys. Chem. B 114, 557 (2010). 10.1021/jp9084926
18. Q. Shao, Y. B. Fan, L. J. Yang, and Y. Q. Gao, J. Chem. Phys. 136, 115101 (2012). 10.1063/1.3692801
19. N. Chennamsetty, V. Voynov, V. Kayser, B. Helk, and B. L. Trout, Proc. Natl. Acad. Sci. U.S.A. 106, 11937 (2009). 10.1073/pnas.0904191106
20. R. S. Kane, P. Deschatelets, and G. M. Whitesides, Langmuir 19, 2388 (2003). 10.1021/la020737x
21. G. Anand, S. N. Jamadagni, S. Garde, and G. Belfort, Langmuir 26, 9695 (2010). 10.1021/la100363m
22. A. J. Keefe and S. Jiang, Nat. Chem. 4, 59 (2012). 10.1038/nchem.1213
23. M. Silow and M. Oliveberg, J. Mol. Biology 326, 263 (2003). 10.1016/S0022-2836(02)01331-1
24. L. F. Zhi, Y. C. Jiang, Y. S. Wang, M. C. Hu, S. N. Li, and Y. J. Ma, Biotechnol. Prog. 23, 729 (2007). 10.1021/bp070024a
25. S. Jayaraman, D. L. Gantz, and O. Gursky, Biochemistry 43, 5520 (2004). 10.1021/bi036274r
26. A. White and S. Y. Jiang, J Phys. Chem. B 115, 660 (2011). 10.1021/jp1067654
27. Q. Shao, Y He, A. White, and S. Y. Jiang, J. Phys. Chem. B 114, 16625 (2010). 10.1021/jp107272n
28. H. J. C. Berendsen, J. R. Grigera, and T. P. Straatsma, J. Phys. Chem. 91, 6269 (1987). 10.1021/j100308a038
29. W. L. Jorgensen, D. S. Maxwell, and J. TiradoRives, J. Am. Chem. Soc. 118, 11225 (1996). 10.1021/ja9621760
30. W. Humphrey, A. Dalke, and K. Schulten, J. Mol. Graphics 14, 33 (1996). 10.1016/0263-7855(96)00018-5
31. D. Van der Spoel, E. Lindahl, B. Hess, G. Groenhof, A. E. Mark, and H. J. C. Berendsen, J. Comput. Chem. 26, 1701 (2005). 10.1002/jcc.20291
32. U. Essmann, L. Perera, M. L. Berkowitz, T. Darden, H. Lee, and L. G. Pedersen, J. Chem. Phys. 103, 8577 (1995). 10.1063/1.470117
33. H. J. C. Berendsen, J. P. M. Postma, W. F. Vangunsteren, A. Dinola, and J. R. Haak, J. Chem. Phys. 81, 3684 (1984). 10.1063/1.448118
34. S. Nose, J. Chem. Phys. 81, 511 (1984). 10.1063/1.447334
35. W. G. Hoover, Phys. Rev. A 31, 1695 (1985). 10.1103/PhysRevA.31.1695
36. M. Parrinello and A. Rahman, J. Appl. Phys. 52, 7182 (1981). 10.1063/1.328693
37. B. Hess, J. Chem. Theory Comput. 4, 116 (2008). 10.1021/ct700200b
38. A. Luzar and D. Chandler, Nature (London) 379, 55 (1996). 10.1038/379055a0
39. P. Zavodszky, J. Kardos, A. Svingor, and G. A. Petsko, Proc. Natl. Acad. Sci. U.S.A. 95, 7406 (1998). 10.1073/pnas.95.13.7406
40. R. M. Daniel, R. V. Dunn, J. L. Finney, and J. C. Smith, Annu. Rev. Biophys. Biomol. Struct. 32, 69 (2003). 10.1146/annurev.biophys.32.110601.142445
41. K. A. Henzler-Wildman, M. Lei, V. Thai, S. J. Kerns, M. Karplus, and D. Kern, Nature (London) 450, 913 (2007). 10.1038/nature06407
42. A. M. Klibanov, Trends Biotechnol. 15, 97 (1997). 10.1016/S0167-7799(97) 01013-5