Protein fluctuations explored by inelastic neutron scattering and dielectric relaxation spectroscopy
Paper in proceedings, 2008

Glasses, supercooled liquids and proteins share common properties, in particular the existence of an energy landscape and the presence of two types of fluctuations, alpha and beta. While the effect of alpha fluctuations on proteins has been known for a few years, the effect of beta fluctuations has not been fully understood. By comparing neutron-scattering data on the protein myoglobin with beta fluctuations in the hydration shell measured by dielectric relaxation spectroscopy, we show that the internal protein motions are slaved to these fluctuations. We also show that there is no 'dynamical transition' in proteins near 200 K. The rapid increase in the mean-square displacement with temperature in many neutron-scattering experiments can be quantitatively predicted by beta fluctuations in the hydration shell.

dielectric relaxation spectroscopy

protein dynamics

beta fluctuations

no dynamical transitions

inelastic neutron

scattering

hydration shell

Author

G. Chen

Los Alamos National Laboratory

P. W. Fenimore

Los Alamos National Laboratory

H. Frauenfelder

Los Alamos National Laboratory

F. Mezei

Los Alamos National Laboratory

Jan Swenson

Chalmers, Applied Physics, Condensed Matter Physics

R. D. Young

Northern Arizona University

Philosophical Magazine

1478-6435 (ISSN)

Vol. 88 33-35 3877-3883

Subject Categories

Other Engineering and Technologies

DOI

10.1080/14786430802585117

More information

Latest update

4/11/2018