Investigating protein-ligand interactions by solution NMR spectroscopy.
Chemphyschem. 2018 Jan 04;:
Authors: Becker W, Bhattiprolu KC, Gubensäk N, Zangger K
Abstract
Protein-ligand interactions are of fundamental importance in almost all processes in living organisms. The ligands comprise small molecules, drugs or biological macromolecules and their interaction strength varies over several orders of magnitude. Solution NMR spectroscopy offers a large repertoire of techniques to study such complexes. Here we give an overview of the different NMR approaches available. The information they provide ranges from the simple information about the presence of binding or epitope mapping to the complete 3D structure of the complex. NMR spectroscopy is particularly useful for the study of weak interactions and for the screening of binding ligands with atomic resolution.
PMID: 29314603 [PubMed - as supplied by publisher]
[NMR paper] Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
PLoS One. 2017;12(9):e0184487
Authors: Delius J, Frank O, Hofmann T
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is well-established in assessing the binding affinity between...
nmrlearner
Journal club
0
09-09-2017 06:59 PM
[NMR paper] Investigating liquid-liquid phase separation of a monoclonal antibody using solution-state NMR spectroscopy: effect of Arg·Glu and Arg·HCl.
Investigating liquid-liquid phase separation of a monoclonal antibody using solution-state NMR spectroscopy: effect of Arg·Glu and Arg·HCl.
Investigating liquid-liquid phase separation of a monoclonal antibody using solution-state NMR spectroscopy: effect of Arg·Glu and Arg·HCl.
Mol Pharm. 2017 Jun 14;:
Authors: Kheddo P, Bramham JE, Dearman RJ, Uddin S, van der Walle CF, Golovanov AP
Abstract
Liquid-liquid phase separation (LLPS) of monoclonal antibody (mAb) formulations involves spontaneous separation into dense...
nmrlearner
Journal club
0
06-15-2017 03:37 PM
Systematic Identification of Protein–Metabolite Interactions in Complex MetaboliteMixtures by Ligand-Detected Nuclear Magnetic Resonance Spectroscopy
Systematic Identification of Protein–Metabolite Interactions in Complex MetaboliteMixtures by Ligand-Detected Nuclear Magnetic Resonance Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01291/20160425/images/medium/bi-2015-012916_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01291
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/TQ5IVPOPNRw
More...
nmrlearner
Journal club
0
04-26-2016 12:14 PM
[NMR paper] Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Biochemistry. 2016 Apr 11;
Authors: Nikolaev YV, Kochanowski K, Link H, Sauer U, Allain FH
Abstract
Protein-metabolite interactions play a vital role in the regulation of numerous cellular processes. Consequently, identifying such interactions is a key prerequisite for...
nmrlearner
Journal club
0
04-12-2016 09:12 PM
[NMR paper] The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Related Articles The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Biochim Biophys Acta. 2015 Apr 30;
Authors: Assfalg M, Ragona L, Pagano K, D'Onofrio M, Zanzoni S, Tomaselli S, Molinari H
Abstract
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
nmrlearner
Journal club
0
05-06-2015 11:59 AM
[NMR paper] Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Methods Mol Biol. 2015;1229:325-33
Authors: Joseph PR, Poluri KM, Sepuru KM, Rajarathnam K
Abstract
Solution nuclear magnetic resonance (NMR) spectroscopy and, in particular, chemical shift perturbation (CSP) titration experiments are ideally suited for characterizing the binding interface of macromolecular complexes. (1)H-(15) N-HSQC-based CSP studies have...
nmrlearner
Journal club
0
10-19-2014 01:27 PM
[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...
nmrlearner
Journal club
0
06-05-2013 06:53 PM
[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...
Investigating protein-ligand interactions by solution NMR spectroscopy.
Linear Mode
