Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis.

ABSTRACT: NMR relaxation analysis of the mobile residues in globular proteins is sensitive to the form of the experimentally fitted internal autocorrelation function, which is used to represent that motion. Different order parameter representations can precisely fit the same set of ¹⁵N R₁, R₂, and heteronuclear NOE measurements while yielding significantly divergent predictions of the underlying autocorrelation functions, indicating the insufficiency of these experimental relaxation data for assessing which order parameter representation provides the most physically realistic predictions. Molecular dynamics simulations offer an unparalleled capability for discriminating among different order parameter representations to assess which representation can m

SUBMITTER: Anderson JS 

PROVIDER: S-EPMC9009080 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature