Abstract
We present detailed dielectric spectroscopy studies of dynamics in two hydrated proteins, lysozyme and myoglobin. We emphasize the importance of explicit account for possible Maxwell-Wagner (MW) polarization effects in protein powder samples. Combining our data with earlier literature results, we demonstrate the existence of three major relaxation processes in globular proteins. To understand the mechanisms of these relaxations we involve literature data on neutron scattering, simulations and NMR studies. The faster process is ascribed to coupled protein-hydration water motions and has relaxation time similar to 10-50 Ps at room temperature. The intermediate process is similar to 10(2)-10(3) times slower than the faster process and might be strongly affected by MW polarizations. Based on the analysis of data obtained by different experimental techniques and simulations, we ascribe this process to large scale domain-like motions of proteins. The slowest observed process is similar to 10(6)-10(7) times slower than the faster process and has anomalously large dielectric amplitude Delta epsilon similar to 10(2)-10(4). The microscopic nature of this process is not clear, but it seems to be related to the glass transition of hydrated proteins. The presentedresults suggest a general classification of the relaxation processes in hydrated proteins. (c) 2014 Elsevier B.V. All rights reserved.
