Trimethylsilyl tag for probing protein-ligand interactions by NMR.
J Biomol NMR. 2018 Mar 21;:
Authors: Becker W, Adams LA, Graham B, Wagner GE, Zangger K, Otting G, Nitsche C
Abstract
Protein-ligand titrations can readily be monitored with a trimethylsilyl (TMS) tag. Owing to the intensity, narrow line shape and unique chemical shift of a TMS group, dissociation constants can be determined from straightforward 1D 1H-NMR spectra not only in the fast but also in the slow exchange limit. The tag is easily attached to cysteine residues and a sensitive reporter of ligand binding also at sites where it does not interfere with ligand binding or catalytic efficiency of the target protein. Its utility is demonstrated for the Zika virus NS2B-NS3 protease and the human prolyl isomerase FK506 binding protein.
PMID: 29564580 [PubMed - as supplied by publisher]
Trimethylsilyl tag for probing proteinā??ligand interactions by NMR
Trimethylsilyl tag for probing proteinā??ligand interactions by NMR
Abstract
Proteinā??ligand titrations can readily be monitored with a trimethylsilyl (TMS) tag. Owing to the intensity, narrow line shape and unique chemical shift of a TMS group, dissociation constants can be determined from straightforward 1D 1H-NMR spectra not only in the fast but also in the slow exchange limit. The tag is easily attached to cysteine residues and a sensitive reporter of ligand binding also at sites where it does not interfere with ligand binding or catalytic...
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03-21-2018 04:04 PM
[NMR paper] Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
Related Articles Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
J Med Chem. 2017 Sep 14;:
Authors: Geist L, Mayer M, Cockcroft XL, Wolkerstorfer B, Kessler D, Engelhardt H, McConnell DB, Konrat R
Abstract
Fragment-based drug design exploits initial screening of low molecular weight compounds and their concomitant affinity improvement. The multitude of possible chemical...
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09-15-2017 08:41 PM
[NMR paper] Overview of Probing Protein-Ligand Interactions Using NMR.
Overview of Probing Protein-Ligand Interactions Using NMR.
Overview of Probing Protein-Ligand Interactions Using NMR.
Curr Protoc Protein Sci. 2015;81:17.18.1-17.18.24
Authors: Aguirre C, Cala O, Krimm I
Abstract
Nuclear magnetic resonance (NMR) is a powerful technique for the study and characterization of protein-ligand interactions. In this unit we review both experiments where the NMR spectrum of the protein is observed (protein-observed NMR experiments) and those where the NMR spectra of the ligand is observed...
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08-04-2015 03:00 PM
[NMR paper] Probing Protein Quinary Interactions by in-cell NMR.
Probing Protein Quinary Interactions by in-cell NMR.
Related Articles Probing Protein Quinary Interactions by in-cell NMR.
Biochemistry. 2015 Apr 20;
Authors: Majumder S, Xue J, DeMott CM, Reverdatto S, Burz DS, Shekhtman A
Abstract
Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, protein weak (quinary) interactions are an emergent property of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro....
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04-22-2015 03:33 PM
[NMR paper] Probing the binding entropy of ligand-protein interactions by NMR.
Probing the binding entropy of ligand-protein interactions by NMR.
Related Articles Probing the binding entropy of ligand-protein interactions by NMR.
Chembiochem. 2005 Sep;6(9):1585-91
Authors: Homans SW
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12-01-2010 06:56 PM
[NMR paper] NMR probing of protein-protein interactions using reporter ligands and affinity tags.
NMR probing of protein-protein interactions using reporter ligands and affinity tags.
Related Articles NMR probing of protein-protein interactions using reporter ligands and affinity tags.
J Am Chem Soc. 2004 Feb 18;126(6):1636-7
Authors: Ludwiczek ML, Baminger B, Konrat R
A novel method is proposed for the detection and quantification of protein-protein interactions in solution. In this approach, one protein binding partner is tagged with a ligand binding domain, and protein-protein interaction is monitored via changes in the NMR relaxation...
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11-24-2010 09:25 PM
[NMR paper] Probing the kinetic landscape of transient peptide-protein interactions by use of pep
Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
Related Articles Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
J Am Chem Soc. 2003 Oct 15;125(41):12432-42
Authors: Tolkatchev D, Xu P, Ni F
Protein-ligand interactions may lead to the formation of multiple...
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11-24-2010 09:16 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...