Structure determination of protein-ligand complexes by NMR in solution
Structure determination of protein-ligand complexes by NMR in solution
Publication date: Available online 8 February 2018
Source:Methods</br>
Author(s): Julien Orts, Alvar D. Gossert</br>
In this paper, we discuss methods for determining structures of protein-ligand complexes by NMR in solution. Our discussion is based on small ligands (<2 kDa) as for example drugs, metabolites or oligo-peptides, but most of the considerations also apply to more general cases. In NMR in solution, the kinetics of association and dissociation of the complex – the exchange rate –...
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[NMR paper] Structure determination of protein-ligand complexes by NMR in solution.
Structure determination of protein-ligand complexes by NMR in solution.
Structure determination of protein-ligand complexes by NMR in solution.
Methods. 2018 Feb 07;:
Authors: Orts J, Gossert AD
Abstract
In this paper, we discuss methods for determining structures of protein-ligand complexes by NMR in solution. Our discussion is based on small ligands (< 2 kDa) as for example drugs, metabolites or oligo-peptides, but most of the considerations also apply to more general cases. In NMR in solution, the kinetics of association and...
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02-11-2018 11:50 AM
[NMR paper] NMR solution structure determination of large RNA-protein complexes.
NMR solution structure determination of large RNA-protein complexes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif NMR solution structure determination of large RNA-protein complexes.
Prog Nucl Magn Reson Spectrosc. 2016 Nov;97:57-81
Authors: Yadav DK, Lukavsky PJ
Abstract
Structure determination of RNA-protein complexes is essential for our understanding of the multiple layers of RNA-mediated posttranscriptional regulation of gene expression. Over the...
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11-29-2016 12:57 AM
NMR solution structure determination of large RNA-protein complexes
NMR solution structure determination of large RNA-protein complexes
Publication date: November 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 97</br>
Author(s): Deepak Kumar Yadav, Peter J. Lukavsky</br>
Structure determination of RNA-protein complexes is essential for our understanding of the multiple layers of RNA-mediated posttranscriptional regulation of gene expression. Over the past 20years, NMR spectroscopy became a key tool for structural studies of RNA-protein interactions. Here, we review the progress being made in NMR structure...
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11-19-2016 08:35 PM
[NMR paper] Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.
Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.
Related Articles Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.
J Am Chem Soc. 2015 Aug 21;
Authors: Eletsky A, Pulavarti SV, Beaumont V, Gollnick P, Szyperski T
Abstract
NMR residual dipolar couplings (RDCs) are exquisite probes of protein structure and dynamics. A new solution NMR experiment named 2D SE2 J-TROSY is presented to...
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08-22-2015 11:20 AM
[NMR paper] Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Related Articles Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Methods Enzymol. 2015;558:279-331
Authors: Duss O, Yulikov M, Allain FH, Jeschke G
Abstract
Although functional significance of large noncoding RNAs and their complexes with proteins is well recognized, structural information for this class of systems is very scarce. Their inherent flexibility causes problems in...
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06-13-2015 11:09 PM
Fast methionine-based solution structure determination of calcium-calmodulin complexes
Fast methionine-based solution structure determination of calcium-calmodulin complexes
Abstract Here we present a novel NMR method for the structure determination of calcium-calmodulin (Ca2+-CaM)-peptide complexes from a limited set of experimental restraints. A comparison of solved CaM-peptide structures reveals invariability in CaMâ??s backbone conformation and a structural plasticity in CaMâ??s domain orientation enabled by a flexible linker. Knowing this, the collection and analysis of an extensive set of NOESY spectra is redundant. Although RDCs can define CaM domain orientation in...