Cross relaxation at the lysozyme–water interface: an NMR line-shape-relaxation correlation study

Abstract

In wet hen egg white lysozyme (HEWL), the molecular dynamics at the lysozyme–water interface was studied using a proton NMR line-shape-relaxation correlation approach that employed selective inversion of the proton magnetization. The intrinsic lysozyme proton spin-lattice relaxation rate, the intrinsic water proton spin-lattice relaxation rate, and the lysozyme proton – water proton cross-relaxation rate were determined. The lysozyme proton – water proton intermolecular interaction couples these protons and contributes to spin-lattice relaxation as well. The results suggest that a minimum of three different correlation times are needed to characterize the water molecule dynamics in wet HEWL.