Rapid Interpretation of Protein Backbone Rotation Dynamics Directly from Spin Relaxation Data.

ABSTRACT: Besides their structure, dynamics is pivotal for protein functions, particularly for intrinsically disordered proteins (IDPs) that do not fold into a fixed 3D structure. However, the detection of protein dynamics is difficult for IDPs and other disordered biomolecules. NMR spin relaxation rates are sensitive to the rapid rotations of chemical bonds, but their interpretation is arduous for IDPs or molecular assemblies with a complex dynamic landscape. Here we demonstrate numerically that the dynamics of a wide range of proteins, from short peptides to partially disordered proteins and peptides in micelles, can be characterized by calculating the total effective correlation times of protein backbone N-H bond rotations, τ_eff, from experimentally measured transverse ¹⁵N s

SUBMITTER: Nencini R 

PROVIDER: S-EPMC11480883 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature