Rotational Dynamics of Proteins from Spin Relaxation Times and Molecular Dynamics Simulations.

ABSTRACT: Conformational fluctuations and rotational tumbling of proteins can be experimentally accessed with nuclear spin relaxation experiments. However, interpretation of molecular dynamics from the experimental data is often complicated, especially for molecules with anisotropic shape. Here, we apply classical molecular dynamics simulations to interpret the conformational fluctuations and rotational tumbling of proteins with arbitrarily anisotropic shape. The direct calculation of spin relaxation times from simulation data did not reproduce the experimental data. This was successfully corrected by scaling the overall rotational diffusion coefficients around the protein inertia axes with a constant factor. The achieved good agreement with experiments allowed the interpretation of the internal and

SUBMITTER: Ollila OHS 

PROVIDER: S-EPMC6150695 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature