On the use of (3)J-coupling NMR data to derive structural information on proteins
Open access
Date
2021-01Type
- Journal Article
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 ensemble compatible with the experimental data can be obtained using this technique, and that accounting for averaging and the ability of the algorithm to escape from local minima for the torsional angle induced by the Karplus relation, are essential for a comprehensive use of 3J-coupling data in protein structure determination. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000469335Publication status
publishedExternal links
Journal / series
Journal of Biomolecular NMRVolume
Pages / Article No.
Publisher
SpringerSubject
Structure refinement; Nuclear magnetic resonance; (3)J-couplings; Averaging time; Restraining force; Conformational sampling; Local-elevation samplingOrganisational unit
03304 - Van Gunsteren, Wilfred F. (emeritus)
More
Show all metadata