The influence of water on protein properties

Journal of Chemical Physics

Volumn 141, Issue 16, 2014, Pages

  Mallamace, Francesco ^a,b,c,d   Baglioni, Piero ^e   Corsaro, Carmelo ^a   Chen, Sow Hsin ^b   Mallamace, Domenico ^a   Vasi, Cirino ^d   Stanley, H Eugene ^c  

^a UNIVERSITY OF MESSINA   (Italy)

^b Massachusetts Institute of Technology Cambridge   (United States)

^c Boston University   (United States)

^d CNR   (Italy)

^e UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENCE OF WATER; BENDING MODES; BIOCHEMICAL ACTIVITY; BOND COUPLING; DYNAMIC TRANSITIONS; FOLDING PROCESS; HYDRATION LEVELS; HYDRATION WATER; LOW-TEMPERATURE REGIME; PROPERTY;

FOURIER SERIES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GLASS; HYDRATION; HYDROGEN BONDS; LIQUIDS; PEPTIDES; TEMPERATURE;

GLASS TRANSITION;

PROTEIN; WATER;

CHEMISTRY; HYDROGEN BOND; INFRARED SPECTROSCOPY; PRESSURE; PROTEIN FOLDING; TEMPERATURE;

HYDROGEN BONDING; PRESSURE; PROTEIN FOLDING; PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; WATER;

EID: 84908428754     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.4900500     Document Type: Article

References (54)

1. P. G. Debenedetti and H. E. Stanley, " Supercooled and glassy water," Phys. Today 56, 40-46 (2003). 10.1063/1.1595053
2. Y. Levy and J. N. Onuchic, Annu. Rev. Biophys. Biomol. Struct. 35, 389-415 (2006). 10.1146/annurev.biophys.35.040405.102134
3. G. A. Jeffrey and W. Saenger, Hydrogen Bonding in Biological Structures (Springer-Verlag, Berlin, 1991).
4. S. H. Chen et al., Proc. Natl. Acad. Sci. U.S.A. 103, 12974-12978 (2006). 10.1073/pnas.0603253103
5. F. Mallamace et al., Proc. Natl. Acad. Sci. U.S.A. 104, 424-428 (2007). 10.1073/pnas.0607138104
6. L. Xu et al., Nat. Phys. 5, 565-569 (2009). 10.1038/nphys1328
7. F. Mallamace et al., Proc. Natl. Acad. Sci. U.S.A. 107, 22457-22462 (2010). 10.1073/pnas.1015340107
8. S. Yip and M. P. Short, Nat. Mater. 12, 774-777 (2013). 10.1038/nmat3746
9. F. Mallamace, C. Corsaro, H. E. Stanley, and S.-H. Chen, Eur. Phys. J. E 34, 94 (2011). 10.1140/epje/i2011-11094-7
10. J. C. Martinez-Garcia, J. Martinez-Garcia, S. J. Rzoska, and J. Hulliger, J. Chem. Phys. 137, 064501 (2012). 10.1063/1.4739750
11. T. Hecksher, A. I. Nielsen, N. Boye Olsen, and J. C. Dyre, Nat. Phys. 4, 737-741 (2008). 10.1038/nphys1033
12. J. C. Mauro, Y. Yue, A. J. Ellison, P. K. Gupta, and D. C. Allan, Proc. Natl. Acad. Sci. U.S.A. 106, 19780-19784 (2009). 10.1073/pnas.0911705106
13. K. T. Wikfeldt, A. Nilsson, and L. G. M. Pettersson, Phys. Chem. Chem. Phys. 13, 19918-19924 (2011). 10.1039/c1cp22076d
14. P. Kumar, K. T. Wikfeldt, D. Schlesinger, L. G. M. Pettersson, and H. E. Stanley, Sci. Rep. 3, 1980 (2013). 10.1038/srep01980
15. S.-H. Chen et al., J. Phys.: Condens. Matter 21, 504102 (2009). 10.1088/0953-8984/21/50/504102
16. A. Paciaroni, A. R. Bizzarri, and S. Cannistaro, Phys. Rev. E 60, R2476 (R) (1999). 10.1103/PhysRevE.60.R2476
17. G. Schiro, F. Natali, and A. Cupane, Phys. Rev. Lett. 109, 128102 (2012). 10.1103/PhysRevLett.109.128102
18. F. H. Stillinger, Science 267, 1935-1939 (1995). 10.1126/science.267.5206.1935
19. S. H. Chen et al., Proc. Natl. Acad. Sci. U.S.A. 103, 9012-9016 (2006). 10.1073/pnas.0602474103
20. X. Q. Chu et al., J. Phys. Chem. B 113, 5001-5006 (2009). 10.1021/jp900557w
21. G. Caliskan et al., J. Am. Chem. Soc. 128, 32-33 (2006). 10.1021/ja056444i
22. M. Lagi et al., J. Phys. Chem. B 112, 1571-1575 (2008). 10.1021/jp710714j
23. M. F. Fomina, G. Schiro, and A. Cupane, Biophys. Chem. 185, 25-31 (2014). 10.1016/j.bpc.2013.11.004
24. K. L. Ngai, S. Capaccioli, and A. Paciaroni, Chem. Phys. 424, 37-44 (2013). 10.1016/j.chemphys.2013.05.018
25. G. Schirò, V. Vetri, C. B. Andersen, F. Natali, M. M. Koza, M. Leone, and A. Cupane, J. Phys. Chem. B 118, 2913-2923 (2014). 10.1021/jp412277y
26. W. Doster, S. Busch, A. M. Gaspar, M.-S. Appavou, J. Wuttke, and H. Scheer, Phys. Rev. Lett. 104, 098101 (2010). 10.1103/PhysRevLett.104.098101
27. M. Rosenstihl and M. Vogel, J. Chem. Phys. 135, 164503 (2011). 10.1063/1.3653943
28. F. H. Stillinger, J. Chem. Phys. 88, 7818-7825 (1988). 10.1063/1.454295
29. H. Frauenfelder, G. A. Petsko, and D. Tsernoglou, Nature 280, 558-563 (1979). 10.1038/280558a0
30. I. E. T. Iben et al., Phys. Rev. Lett. 62, 1916-1919 (1989). 10.1103/PhysRevLett.62.1916
31. F. Parak and E. W. Knapp, Proc. Natl. Acad. Sci. U.S.A. 81, 7088-7092 (1984). 10.1073/pnas.81.22.7088
32. G. Zaccai, " How soft is a protein ?" Science 288, 1604-1607 (2000). 10.1126/science.288.5471.1604
33. B. F. Rasmussen, A. M. Stock, D. Ringe, and G. A. Petsko, Nature 357, 423-424 (1992). 10.1038/357423a0
34. J. A. Rupley and G. Careri, " Protein hydration and function," Adv. Protein Chem. 41, 37-172 (1991). 10.1016/S0065-3233(08)60197-7
35. W. Doster, S. Cusack, and W. Petry, Nature 337, 754-756 (1989). 10.1038/337754a0
36. M. Ferrand, A. J. Dianoux, W. Petry, and G. Zaccai, Proc. Natl. Acad. Sci. U.S.A. 90, 9668-9672 (1993). 10.1073/pnas.90.20.9668
37. G. Careri, Prog. Biophys. Mol. Biol. 70, 223-249 (1998). 10.1016/S0079-6107(98)00030-3
38. L. Pauling, R. B. Corey, and H. R. Branson, Proc. Natl. Acad. Sci. U.S.A. 37, 205-211 (1951). 10.1073/pnas.37.4.205
39. D. Russo, G. L. Hura, and J. R. D. Copley, Phys. Rev. E 75, 040902 (2007). 10.1103/PhysRevE.75.040902
40. M. Tarek and D. J. Tobias, Phys. Rev. Lett. 88, 138101 (2002). 10.1103/PhysRevLett.88.138101
41. J. T. Pelton and L. R. McLean, Anal. Biochem. 277, 167-176 (2000). 10.1006/abio.1999.4320
42. G. E. Walrafen, M. R. Fisher, M. S. Hokomabadi, and W. H. Yang, J. Chem. Phys. 85, 6970-6982 (1986). 10.1063/1.451384
43. S. Adams, A. M. Higgins, and R. A. L. Jones, Langmuir 18, 4854-4861 (2002). 10.1021/la0112413
44. E. S. Eberhardt and R. T. Raines, J. Am. Chem. Soc. 116, 2149-2150 (1994). 10.1021/ja00084a067
45. S. T. R. Walsh et al., Protein Sci. 12, 520-531 (2003). 10.1110/ps.0223003
46. A. Cooper, Biophys. Chem. 115, 89-97 (2005). 10.1016/j.bpc.2004.12.011
47. M. Sundaralingam and Y. C. Serkharudu, Science 244, 1333-1337 (1989). 10.1126/science.2734612
48. R. Gilmanshin, S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer, Proc. Natl. Acad. Sci. U.S.A. 94, 3709-3713 (1997). 10.1073/pnas.94.8.3709
49. F. Mallamace et al., J. Phys. Chem. B 114, 1870-1878 (2010). 10.1021/jp910038j
50. F. Mallamace et al., J. Chem. Phys. 139, 214502 (2013). 10.1063/1.4833595
51. O. F. A. Larsen and S. Woutersen, J. Chem. Phys. 121, 12143-12145 (2004). 10.1063/1.1839175
52. F. Mallamace et al., Proc. Natl. Acad. Sci. U.S.A. 104, 18387-18391 (2007). 10.1073/pnas.0706504104
53. J. D. Eaves, C. J. Fecko, A. L. Stevens, P. Peng, and A. Tokmakoff, Chem. Phys. Lett. 376, 20-25 (2003). 10.1016/S0009-2614(03)00890-X
54. T. Blundell, D. Barlow, N. Borkakoti, and J. Thornton, Nature 306, 281-283 (1983). 10.1038/306281a0