[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...
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03-25-2015 10:15 AM
Using Chemical Shift Perturbation to Characterise Ligand Binding
Using Chemical Shift Perturbation to Characterise Ligand Binding
Available online 21 March 2013
Publication year: 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
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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 added, and uses these to determine the location of the binding site, the affinity of the ligand, and/or possibly the structure of the complex. A key factor in determining the appearance of spectra during...
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03-21-2013 02:58 PM
Accuracy and precision of proteinâ??ligand interaction kinetics determined from chemical shift titrations
Accuracy and precision of proteinâ??ligand interaction kinetics determined from chemical shift titrations
Abstract NMR-monitored chemical shift titrations for the study of weak proteinâ??ligand interactions represent a rich source of information regarding thermodynamic parameters such as dissociation constants (K D ) in the micro- to millimolar range, populations for the free and ligand-bound states, and the kinetics of interconversion between states, which are typically within the fast exchange regime on the NMR timescale. We recently developed two chemical shift titration methods...
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10-24-2012 10:28 PM
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
J Mol Graph Model. 2011 Sep 3;
Authors: Fukunishi Y, Mizukoshi Y, Takeuchi K, Shimada I, Takahashi H, Nakamura H
Abstract
We developed a new protein-ligand docking calculation method using experimental NMR data. Recently, we proposed a novel ligand epitope-mapping experiment, which utilizes the difference between the longitudinal relaxation rates of ligand protons with and...
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09-24-2011 04:11 PM
[NMR paper] Ligand-induced structural changes to maltodextrin-binding protein as studied by solut
Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy.
Related Articles Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy.
J Mol Biol. 2001 Jun 15;309(4):961-74
Authors: Evenäs J, Tugarinov V, Skrynnikov NR, Goto NK, Muhandiram R, Kay LE
Solution NMR studies on the physiologically relevant ligand-free and maltotriose-bound states of maltodextrin-binding protein (MBP) are presented. Together with existing data on MBP in complex with...
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11-19-2010 08:32 PM
[NMR paper] Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dime
Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Related Articles Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Prog Biophys Mol Biol. 1994;62(2):153-84
Authors: Clore GM, Gronenborn AM
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[NMR paper] Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dime
Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Related Articles Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Prog Biophys Mol Biol. 1994;62(2):153-84
Authors: Clore GM, Gronenborn AM
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[NMR paper] On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase a
On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
Related Articles On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
J Biochem. 1991 Jan;109(1):144-9
Authors: Fujii S, Nonaka Y, Okamoto M, Miura R
The interaction between 2',5'-ADP and NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria was examined by titrating the enzyme with...
Using Ligand-Induced Protein Chemical Shift PerturbationsTo Determine Protein–Ligand Structures
Linear Mode
