General features of proton longitudinal relaxation in proteins in solution

Abstract

Time courses of the recovery upon nonselective inversion of all individual proton magnetizations in several globular proteins in aqueous ( 2H 2O) solution were calculated for varying degrees of rotational correlation time of the molecule (10 −9 s ∼ ∞) and compared with the experimental data on various proteins at 400 MHz. In the calculation, the spinrelaxation mechanism was assumed to be solely the dipolar interaction between protons, and the three-site random jumps of the methyl groups, along with the rotation of the whole molecule, were taken into account. The following conclusions were drawn. ( 1 ) For proteins whose molecular weights are below ∼ 10,000, whole-molecule rotation is a dominant source of relaxation, and the longitudinal relaxation times may vary considerably from proton to proton. (2) For proteins whose molecular weights are above ∼20,000, methyl group rotations assisted by spin diffusion are common and major sources of relaxation, producing T 1 values close to 1 s. In the intermediate region (molecular weight 10,000 ∼ 20,000), both whole-molecule rotation and methyl group rotations contribute significantly to relaxation. (3) In some proteins, segmental motions are as important as methyl group rotations in determining relaxation rate.