Picosecond-time-scale fluctuations of proteins in glassy matrices: the role of viscosity.
Through elastic neutron scattering we investigated the fast dynamics of lysozyme in hydrated powder form or embedded in glycerol-water and glucose-water matrices. We calculated the relaxational contribution to the mean square displacements of protein hydrogen atoms. We found that the inverse of this quantity is linearly proportional to the logarithm of the viscosity of the solvent glassy matrix. This relationship suggests a close connection between the picosecond-time-scale dynamics of protein side chains and the solvent structural relaxation.
Cornicchi
Elena
E
Dipartimento di Fisica, Università di Perugia, INFM-CRS SOFT Unità di Perugia, and Centro per i Materiali Innovativi e Nanostrutturati (CEMIN), Via A. Pascoli, I-06123 Perugia, Italy.
Onori
Giuseppe
G
Paciaroni
Alessandro
A
D003198:Computer Simulation; D005947:Glucose / Q000737:chemistry*; D005990:Glycerol / Q000737:chemistry*; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D044367:Phase Transition; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D013997:Time Factors; D014783:Viscosity; D014867:Water / Q000737:chemistry*
D011506:Proteins; D012997:Solvents; D014867:Water; D009113:Muramidase; D005947:Glucose; D005990:Glycerol