title: Low-frequency vibrational properties of lysozyme in sugar aqueous solutions: a Raman scattering and molecular dynamics simulation study.
abstract: The low-frequency (omega<400 cm(-1)) vibrational properties of lysozyme in aqueous solutions of three well-known protecting sugars, namely, trehalose, maltose, and sucrose, have been investigated by means of complementary Raman scattering experiments and molecular dynamics simulations. The comparison of the Raman susceptibility chi(")(omega) of lysozyme/water and lysozyme/sugar/water solutions at a concentration of 40 wt % with the chi(") of dry lysozyme suggests that the protein dynamics mostly appears in the broad peak around 60-80 cm(-1) that reflects the vibrations experienced by atoms within the cage formed by their neighbors, whereas the broad shoulder around 170 cm(-1) mainly stems from the intermolecular O-H...O stretching vibrations of water. The addition of sugars essentially induces a significant high frequency shift and intensity reduction of this band that reveal a slowing down of water dynamics and a distortion of the tetrahedral hydrogen bond network of water, respectively. Furthermore, the lysozyme vibrational densities of states (VDOS) have been determined from simulations of lysozyme in 37-60 wt % disaccharide aqueous solutions. They exhibit an additional broad peak around 290 cm(-1), in line with the VDOS of globular proteins obtained in neutron scattering experiments. The influence of sugars on the computed VDOS mostly appears on the first peak as a slight high-frequency shift and intensity reduction in the low-frequency range (omega<50 cm(-1)), which increase with the sugar concentration and with the exposition of protein residues to the solvent. These results suggest that sugars stiffen the environment experienced by lysozyme atoms, thereby counteracting the softening of protein vibrational modes upon denaturation, observed at high temperature in the Raman susceptibility of the lysozyme/water solution and in the computed VDOS of unfolded lysozyme in water. Finally, the Raman susceptibility of sugar/water solutions and the calculated VDOS of water in the different lysozyme solutions confirm that sugars induce a significant strengthening of the hydrogen bond network of water that may stabilize proteins at high temperatures.
authors.affiliation: Laboratoire de Dynamique et Structure des Matériaux Moléculaires, UMR CNRS 8024, Université Lille I, 59655 Villeneuve d'Ascq Cedex, France. alerbret@yahoo.com
authors.forename: A
authors.initials: A
authors.lastname: Lerbret
authors.forename: F
authors.initials: F
authors.lastname: Affouard
authors.forename: P
authors.initials: P
authors.lastname: Bordat
authors.forename: A
authors.initials: A
authors.lastname: Hédoux
authors.forename: Y
authors.initials: Y
authors.lastname: Guinet
authors.forename: M
authors.initials: M
authors.lastname: Descamps
mesh_terms: D000818:Animals; D002241:Carbohydrates / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D012996:Solutions; D013059:Spectrum Analysis, Raman; D014732:Vibration; D014867:Water / Q000737:chemistry*
chemical_list: D002241:Carbohydrates; D012996:Solutions; D014867:Water; D009113:Muramidase