[NMR paper] On the use of time-averaging restraints when deriving biomolecular structure from [Formula: see text]-coupling values obtained from NMR experiments.
Related ArticlesOn the use of time-averaging restraints when deriving biomolecular structure from [Formula: see text]-coupling values obtained from NMR experiments.
J Biomol NMR. 2016 Sep 15;
Authors: Smith LJ, van Gunsteren WF, Hansen N
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.
PMID: 27627888 [PubMed - as supplied by publisher]
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
J Am Chem Soc. 2011 Apr 4;
Authors: Ryabov Y, Schwieters CD, Clore GM
(15)N R(2)/R(1) relaxation data contain information on molecular shape and size as well as on bond vector orientations relative to...
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04-06-2011 10:54 AM
Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Yaroslav Ryabov, Charles D. Schwieters and G. Marius Clore
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201020c/aop/images/medium/ja-2011-01020c_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201020c
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04-05-2011 10:37 AM
Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.
Hydrodynamic dispersion in -lactoglobulin gels measured by PGSE NMR.
Hydrodynamic dispersion in -lactoglobulin gels measured by PGSE NMR.
Eur Phys J E Soft Matter. 2011 Feb;34(2):1-15
Authors: Fridjonsson EO, Bernin D, Seymour JD, Nydén M, Codd SL
The displacement scale dependent molecular dynamics of solvent water molecules flowing through -lactoglobulin gels are measured by pulse gradient spin echo (PGSE) nuclear magnetic resonance (NMR). Gels formed under different p H conditions generate structures which are characterized by magnetic...
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03-02-2011 11:54 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
J Am Chem Soc. 2011 Feb 2;
Authors: Shi L, Traaseth NJ, Verardi R, Gustavsson M, Gao J, Veglia G
Residual dipolar couplings (RDCs) are widely used as orientation-dependent NMR restraints to improve the resolution of the NMR conformational ensemble of biomacromolecules and define the...
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02-04-2011 11:34 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Lei Shi, Nathaniel J. Traaseth, Raffaello Verardi, Martin Gustavsson, Jiali Gao and Gianluigi Veglia
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109080t/aop/images/medium/ja-2010-09080t_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109080t
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[NMR paper] On deriving spatial protein structure from NMR or X-ray diffraction data.
On deriving spatial protein structure from NMR or X-ray diffraction data.
Related Articles On deriving spatial protein structure from NMR or X-ray diffraction data.
Ciba Found Symp. 1991;161:150-9; discussion 159-66
Authors: van Gunsteren WF, Gros P, Torda AE, Berendsen HJ, van Schaik RC
During the last decade it has become possible to derive the spatial structure of small proteins in solution using multidimensional NMR spectroscopy measurements and interpreting the data in terms of a chemical atomic model. The NMR experiments generate a set...
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On the use of time-averaging restraints when deriving biomolecular structure from [Formula: see text]-coupling values obtained from NMR experiments.
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