On the use of ³J-coupling NMR data to derive structural information on proteins.

ABSTRACT: Values of ³J-couplings as obtained from NMR experiments on proteins cannot easily be used to determine protein structure due to the difficulty of accounting for the high sensitivity of intermediate ³J-coupling values (4-8 Hz) to the averaging period that must cover the conformational variability of the torsional angle related to the ³J-coupling, and due to the difficulty of handling the multiple-valued character of the inverse Karplus relation between torsional angle and ³J-coupling. Both problems can be solved by using ³J-coupling time-averaging local-elevation restraining MD simulation. Application to the protein hen egg white lysozyme using 213 backbone and side-chain ³J-coupling restraints shows that a conformational ens

SUBMITTER: Smith LJ 

PROVIDER: S-EPMC7897194 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature