Temperature-dependent dynamics at protein-solvent interfaces.

Abstract

We perform differential scanning calorimetry, broadband dielectric spectroscopy (BDS), and nuclear magnetic resonance (NMR) studies to understand the molecular dynamics in mixtures of ethylene glycol with elastin or lysozyme over broad temperature ranges. To focus on the protein-solvent interface, we use mixtures with about equal numbers of amino acids and solvent molecules. The elastin and lysozyme mixtures show similar glass transition steps, which extend over a broad temperature range of 157-185K. The BDS and NMR studies yield fully consistent results for the fastest process P1, which is caused by the structural relaxation of ethylene glycol between the protein molecules and follows an Arrhenius law with an activation energy of Ea = 0.63eV. It involves quasi-isotropic reorientation and is very similar in the elastin and lysozyme matrices but different from the α and β relaxations of bulk ethylene glycol. Two slower BDS processes, viz., P2 and P3, have protein-dependent time scales, but they exhibit a similar Arrhenius-like temperature dependence with an activation energy of Ea ∼ 0.81eV. However, P2 and P3 do not have a clear NMR signature. In particular, the NMR results for the lysozyme mixture reveal that the protein backbone does not show isotropic α-like motion on the P2 and P3 time scales but only restricted β-like reorientation. The different activation energies of the P1 and P2/P3 processes do not support an intimate coupling of protein and ethylene glycol dynamics. The present results are compared with previous findings for mixtures of proteins with water or glycerol, implying qualitatively different dynamical couplings at various protein-solvent interfaces.