[NMR paper] On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking.
On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking.
Related Articles On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking.
J Chem Inf Model. 2015 Jul 30;
Authors: Onila I, Ten Brink T, Fredriksson K, Codutti L, Mazur A, Griesinger C, Carlomagno T, Exner TE
Abstract
INPHARMA (Internuclear NOEs for Pharmacophore Mapping) determines the relative orientation of two competitive ligands in the protein binding pocket. It is based on the...
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[NMR paper] Analysis of ligand-protein exchange by Clustering of Ligand Diffusion Coefficient Pairs (CoLD-CoP)
Analysis of ligand-protein exchange by Clustering of Ligand Diffusion Coefficient Pairs (CoLD-CoP)
Publication date: Available online 23 March 2015
Source:Journal of Magnetic Resonance</br>
Author(s): David S. Snyder , Mihaela Chantova , Saadia Chaudhry</br>
NMR spectroscopy is a powerful tool in describing protein structures and protein activity for pharmaceutical and biochemical development. This study describes a method to determine weak binding ligands in biological systems by using hierarchic diffusion coefficient clustering of multidimensional data obtained...
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Abstract We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By...
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[NMR paper] Analysis of protein/ligand interactions with NMR diffusion measurements: the importan
Analysis of protein/ligand interactions with NMR diffusion measurements: the importance of eliminating the protein background.
Related Articles Analysis of protein/ligand interactions with NMR diffusion measurements: the importance of eliminating the protein background.
J Magn Reson. 2002 Apr;155(2):217-25
Authors: Derrick TS, McCord EF, Larive CK
Pulsed-field gradient nuclear magnetic resonance (PFG-NMR) is a well-established method for the determination of translational diffusion coefficients. Recently, this method has found applicability in...