Using chemical shift perturbation to characterise ligand binding

MP Williamson - Progress in nuclear magnetic resonance spectroscopy, 2013 - Elsevier
Chemical shift perturbation (CSP, chemical shift mapping or complexation-induced changes
in chemical shift, CIS) follows changes in the chemical shifts of a protein when a ligand is …

The use of NMR methods for conformational studies of nucleic acids

SS Wijmenga, BNM Van Buuren - Progress in nuclear magnetic resonance …, 1998 - Elsevier
Nucleic acid molecules play a central role in cell biological processes. DNA's main role is to
act as the carrier of genetic information. Furthermore, DNA is transcribed into RNA by a …

Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks

Y Shen, A Bax - Journal of biomolecular NMR, 2013 - Springer
Abstract A new program, TALOS-N, is introduced for predicting protein backbone torsion
angles from NMR chemical shifts. The program relies far more extensively on the use of …

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Y Shen, F Delaglio, G Cornilescu, A Bax - Journal of biomolecular NMR, 2009 - Springer
NMR chemical shifts in proteins depend strongly on local structure. The program TALOS
establishes an empirical relation between 13 C, 15 N and 1 H chemical shifts and backbone …

GROMACS: fast, flexible, and free

D Van Der Spoel, E Lindahl, B Hess… - Journal of …, 2005 - Wiley Online Library
This article describes the software suite GROMACS (Groningen MAchine for Chemical
Simulation) that was developed at the University of Groningen, The Netherlands, in the early …

GROMACS 3.0: a package for molecular simulation and trajectory analysis

E Lindahl, B Hess, D Van Der Spoel - Molecular modeling annual, 2001 - Springer
GROMACS 3.0 is the latest release of a versatile and very well optimized package for
molecular simulation. Much effort has been devoted to achieving extremely high …

Consistent blind protein structure generation from NMR chemical shift data

Y Shen, O Lange, F Delaglio, P Rossi… - Proceedings of the …, 2008 - National Acad Sciences
Protein NMR chemical shifts are highly sensitive to local structure. A robust protocol is
described that exploits this relation for de novo protein structure generation, using as input …

Temperature dependence of 1H chemical shifts in proteins

NJ Baxter, MP Williamson - Journal of biomolecular NMR, 1997 - Springer
Temperature coefficients have been measured by 2D NMR methods forthe amide and CαH
proton chemical shifts in two globularproteins, bovine pancreatic trypsin inhibitor and hen …

De novo protein structure generation from incomplete chemical shift assignments

Y Shen, R Vernon, D Baker, A Bax - Journal of biomolecular NMR, 2009 - Springer
NMR chemical shifts provide important local structural information for proteins. Consistent
structure generation from NMR chemical shift data has recently become feasible for proteins …

Magnetic Field Dependence of Nitrogen−Proton J Splittings in 15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar …

N Tjandra, S Grzesiek, A Bax - Journal of the American Chemical …, 1996 - ACS Publications
One-bond 1 J NH couplings have been measured in 15N-enriched human ubiquitin and
range from 91.1 to 95.6 Hz. Measurements have been carried out using two different …