Vibrational excitations of proteins and their hydration water in the far-infrared range

被引：10

作者：

Paciaroni, A. ^{[1
]}

Nibali, V. Conti ^{[2
]}

Orecchini, A. ^{[1
,3
]}

Petrillo, C. ^{[1
]}

Haertlein, M. ^{[3
]}

Moulin, M. ^{[3
]}

Tarek, M. ^{[4
]}

D'Angelo, G. ^{[5
]}

Sacchetti, F. ^{[1
]}

机构：

[1] Univ Perugia, Dipartimento Fis, I-06123 Perugia, Italy

[2] Ruhr Univ Bochum, Lehrstuhl Phys Chem 2, D-44780 Bochum, Germany

[3] Inst Max Von Laue Paul Langevin, F-38042 Grenoble, France

[4] Nancy Univ, CNRS, UMR Struct & React Syst Mol Complexes, Nancy, France

[5] Univ Messina, Dipartimento Fis, I-98166 Messina, Italy

来源：

CHEMICAL PHYSICS | 2013年 / 424卷

关键词：

Protein dynamics; Vibrational density of states; Inelastic neutron scattering; Molecular dynamics simulations; Maltose binding protein; Biological water; NEUTRON-SCATTERING; MOLECULAR-DYNAMICS; COPPER AZURIN; STATES; SPECTROSCOPY; MYOGLOBIN; ANOMALIES;

D O I：

10.1016/j.chemphys.2013.05.013

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Incoherent neutron scattering has been used to single out the vibrational contribution from maltose binding protein (MBP) and its hydration water in the energy range 1 meV-80 meV. The vibrational density of states from both protein and hydration water have been investigated by measuring respectively dry and D2O-hydrated isotopically natural MBP and dry and H2O-hydrated perdeuterated MBP. Molecular dynamics simulations done on the same system allow us to attribute the protein inelastic features. The inelastic behavior of the biomolecule seems to be largely independent on the presence of solvent. Conversely, protein hydration water exhibits remarkable differences with respect to hexagonal ice in the whole spectral range, with clear similarities to amorphous phases of ice. (C) 2013 Elsevier B. V. All rights reserved.

引用

页码：80 / 83

页数：4

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