Their emerging nature as multifunctional effectors explains the large interest to monitor glycan binding to galectins and to define bound-state conformer(s) of their ligands in solution. Basically, NMR spectroscopy facilitates respective experiments. Towards developing new and even better approaches for these purposes, extending the range of exploitable isotopes beyond ¹H, ^(13)C, and ^(15)N offers promising perspectives. Having therefore prepared selenodigalactoside and revealed its bioactivity...
[NMR paper] Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
Chemistry. 2021 Jan 04;27(1):316-325
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02-18-2021 03:17 PM
[NMR paper] Analyzing multi-step ligand binding reactions for oligomeric proteins by NMR: Theoretical and computational considerations.
Analyzing multi-step ligand binding reactions for oligomeric proteins by NMR: Theoretical and computational considerations.
Analyzing multi-step ligand binding reactions for oligomeric proteins by NMR: Theoretical and computational considerations.
J Magn Reson. 2020 Aug 04;318:106802
Authors: Harkness RW, Toyama Y, Kay LE
Abstract
Solution NMR spectroscopy is widely used to investigate the thermodynamics and kinetics of the binding of ligands to their biological receptors, as it provides detailed, atomistic information,...
[NMR paper] Analyzing organophosphate pesticide-serum albumin binding interaction: A combined STD NMR and molecular docking study.
Analyzing organophosphate pesticide-serum albumin binding interaction: A combined STD NMR and molecular docking study.
Related Articles Analyzing organophosphate pesticide-serum albumin binding interaction: A combined STD NMR and molecular docking study.
J Biomol Struct Dyn. 2020 Mar 19;:1-24
Authors: Dahiya V, Anand BG, Kar K, Pal S
Abstract
In Vitro analysis of the interaction of organophosphate pesticides (OP) with bovine serum albumin (BSA) is crucial to understand their potential effects at the molecular level. In this...
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03-21-2020 12:53 AM
[NMR paper] Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Abstract: The biological recognition of complex-type N-glycans is part of many key physiological and pathological events. Despite their importance, the structural characterization of these events remains an unsolved task. The inherent flexibility of N-glycans hampers crystallization and the chemical equivalence of individual branches precludes their NMR characterization. By using a chemoenzymatically synthesized tetraantennary N-glycan...
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10-09-2017 04:12 PM
[Stan NMR blog] Introducing GSD-2D
Introducing GSD-2D
Presentation of an extension of GSD to two dimensions.
Source: Stan blog library
[NMR paper] Analyzing protein-ligand interactions by dynamic NMR spectroscopy.
Analyzing protein-ligand interactions by dynamic NMR spectroscopy.
Related Articles Analyzing protein-ligand interactions by dynamic NMR spectroscopy.
Methods Mol Biol. 2013;1008:243-66
Authors: Mittermaier A, Meneses E
Abstract
Nuclear magnetic resonance (NMR) spectroscopy can provide detailed information on protein-ligand interactions that is inaccessible using other biophysical techniques. This chapter focuses on NMR-based approaches for extracting affinity and rate constants for weakly binding transient protein complexes with lifetimes...