Study of solvent–protein coupling effects by neutron scattering
Study of solvent–protein coupling effects by neutron scattering
复制标题
通过中子散射研究溶剂-蛋白质耦合效应
DOI:
10.1007/s10867-009-9177-5
复制
发表时间:
2010
影响因子:
1.8
通讯作者:
M. Telling
中科院分区:
文献类型:
--
作者:
Balázs Varga;F. Migliardo;F. Migliardo;E. Takács;Beáta G. Vértessy;S. Magazù;M. Telling
The present work aims to characterize the dynamical behavior of proteins immersed in bio-preserving liquids and glasses. For this purpose, the protein dUTPase was chosen, while the selected solvents were glycerol, a triol, and some homologous disaccharides, i.e., trehalose, maltose, and sucrose, which are known to be very effective bio-preserving agents. The results highlight that the disaccharides show a slowing down effect on the water dynamics, which is stronger for trehalose than in the case of the other disaccharides. Furthermore, a characterization of the medium which hosts the protein is performed by using an operative definition of fragility based on the mean square displacement extracted by elastic incoherent neutron scattering, which is directly connected to Angell’s kinetic fragility based on the viscosity. Finally, a study of the dynamics of the protein sequestered within the solvents is performed. The result shows that the protein dynamics is coupled with that of the surrounding matrix.