journal article·2015-01

Mapping water dynamics in defined local environment: From hindered rotation to vibrational modes

Daniela Russo, José Teixeira

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Abstract

We present insight into the way how vibrational modes of hydration water may be affected by the hydrophilic or hydrophobic nature of protein sites rather than by their curvature. We will illustrate how hydrophobicity promotes a dynamical behaviour similar to that of low density amorphous ice and how it affects the dynamics of the first interacting water molecules. We study the evolution of the hydrogen bond network dynamics as a function of the number of water molecules and explain the origin of the similarities between the dynamics of supercooled and hydration water. Finally we give an insight into the collective dynamics of hydration water and its correlation to the hydrogen bond network around bio-molecules. We discuss hydration dynamics results of our system, as a model of protein, in the context of glassy systems, protein function, folding and stability and protein-protein interfaces, giving a perspective of developments and applications.
Source: openaire · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Material Dynamics and Properties · Protein Structure and Dynamics · Spectroscopy and Quantum Chemical Studies

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

References (28)

Show source-provided references
1. Careri · Proc. Natl. Acad. Sci. U. S. A. · 1986 · 83 · 681010.1073/pnas.83.18.6810 ↗
2. Janin · Struct. Fold. Des. · 1999 · 7 · R27710.1016/S0969-2126(00)88333-1 ↗
3. Fenimore · Proc. Natl. Acad. Sci. U. S. A. · 2002 · 99 · 1604710.1073/pnas.212637899 ↗
4. Hura · Perspect. Drug Discovery Des. · 1999 · 17 · 9710.1023/A:1008778724866 ↗
5. Sorenson · J. Phys. Chem. B · 1999 · 103 · 541310.1021/jp990434k ↗
6. Russo · Biophys. J. · 2004 · 86 · 185210.1016/S0006-3495(04)74252-6 ↗
7. Russo · J. Phys. Chem. B · 2004 · 108 · 1988510.1021/jp046847p ↗
8. Born · J. Am. Chem. Soc. · 2009 · 131 · 375210.1021/ja808997y ↗
9. Boopathi · J. Biomol. Struct. Dyn. · 2013 · 31 · 15810.1080/07391102.2012.698380 ↗
10. Qvist · Faraday Discuss. · 2009 · 141 · 13110.1039/B806194G ↗
11. Mazur · J. Phys. Chem. B · 2010 · 114 · 1068410.1021/jp106423a ↗
12. Ide · J. Phys. Chem. B · 1997 · 101 · 702210.1021/jp971334m ↗
13. Russo · J. Mol. Struct. · 2010 · 972 · 8110.1016/j.molstruc.2009.12.020 ↗
14. Russo · J. Phys. Chem. Chem. Phys. · 2008 · 10 · 496810.1039/b807551b ↗
15. Russo · J. Am. Chem. Soc. · 2011 · 133 · 488210.1021/ja109610f ↗
16. Russo · Chem. Phys. · 2007 · 345 · 20010.1016/j.chemphys.2007.08.001 ↗
17. Russo · Phys. Rev. E. · 2007 · 75 · 04090210.1103/PhysRevE.75.040902 ↗
18. Russo · J. Chem. Phys. · 2009 · 130 · 23510110.1063/1.3154383 ↗
19. Nibali · J. Phys. Chem. Lett. · 2014 · 5 · 118110.1021/jz500023e ↗
20. Heyden · Phys. Rev. Lett. · 2013 · 111 · 21810110.1103/PhysRevLett.111.218101 ↗
21. Russo · J. Spectro. · 2012 · 27 · 29310.1155/2012/671265 ↗
22. Lambreva · Curr. Protein Pept. Sci. · 2014 · 15 · 28510.2174/1389203715666140327104802 ↗
23. Russo · Chem. Phys. · 2003 · 292 · 23510.1016/S0301-0104(03)00200-3 ↗
24. Russo · Chem. Phys. Lett. · 2011 · 517 · 8010.1016/j.cplett.2011.10.031 ↗
25. Teixeira · Phys. Rev. A · 1985 · 31 · 191310.1103/PhysRevA.31.1913 ↗
26. Russo · J. Phys. Chem. B · 2013 · 117 · 282910.1021/jp3094885 ↗
27. Doshi · Proc. Natl. Acad. Sci. U. S. A. · 2005 · 102 · 945810.1073/pnas.0504034102 ↗
28. Khalfa · J. Phys. Chem. B · 2010 · 114 · 267610.1021/jp9064196 ↗