On the Use of Side-Chain NMR Relaxation Data to Derive Structural and Dynamical Information on Proteins: A Case Study Using Hen Lysozyme.

ABSTRACT: Values of S2CH and S2NH order parameters derived from NMR relaxation measurements on proteins cannot be used straightforwardly to determine protein structure because they cannot be related to a single protein structure, but are defined in terms of an average over a conformational ensemble. Molecular dynamics simulation can generate a conformational ensemble and thus can be used to restrain S2CH and S2NH order parameters towards experimentally derived target values S2CH (exp) and S2NH (exp). Application of S2CH and S2NH order-parameter restraining MD simulation to bond vectors in 63 side chains of the protein hen egg white lysozyme using 51 S2CH (exp) target values and 28 S2NH (exp) target values shows that a conformational ensemble compatible with the experimentally derived data can be obt

SUBMITTER: Smith LJ 

PROVIDER: S-EPMC8048695 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature