On the use of time-averaging restraints when deriving biomolecular structure from ³ J -coupling values obtained from NMR experiments

Lorna J Smith; Wilfred F van Gunsteren; Niels Hansen

doi:10.1007/s10858-016-0058-5

On the use of time-averaging restraints when deriving biomolecular structure from ³ J -coupling values obtained from NMR experiments

J Biomol NMR. 2016 Sep;66(1):69-83. doi: 10.1007/s10858-016-0058-5. Epub 2016 Sep 15.

Authors

Lorna J Smith¹, Wilfred F van Gunsteren², Niels Hansen³

Affiliations

¹ Inorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QR, UK.
² Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH, 8093, Zurich, Switzerland.
³ Institute of Thermodynamics and Thermal Process Engineering, University of Stuttgart, 70569, Stuttgart, Germany. hansen@itt.uni-stuttgart.de.

PMID: 27627888
DOI: 10.1007/s10858-016-0058-5

Abstract

Deriving molecular structure from [Formula: see text]-couplings obtained from NMR experiments is a challenge due to (1) the uncertainty in the Karplus relation [Formula: see text] connecting a [Formula: see text]-coupling value to a torsional angle [Formula: see text], (2) the need to account for the averaging inherent to the measurement of [Formula: see text]-couplings, and (3) the sampling road blocks that may emerge due to the multiple-valuedness of the inverse function [Formula: see text] of the function [Formula: see text]. Ways to properly handle these issues in structure refinement of biomolecules are discussed and illustrated using the protein hen egg white lysozyme as example.

Keywords: Conformational dynamics; Force field; Nuclear magnetic resonance; Statistical mechanics; Structure refinement.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Algorithms
Models, Molecular*
Models, Theoretical
Molecular Structure*
Nuclear Magnetic Resonance, Biomolecular* / methods