[NMR paper] Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy
Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy
Saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy is an established technique for detecting and characterizing the binding of small molecules, such as metabolites, to biological macromolecules like proteins and nucleic acids. STD NMR allows detection of binding in complex mixtures of potential ligands, which is often used for library screening in the pharmaceutical industry but may also be beneficial for binding studies with metabolite mixtures. The nature of the...
A COVID moonshot: assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy
A COVID moonshot: assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the etiological cause of the coronavirus disease 2019, for which no effective antiviral therapeutics are available. The SARS-CoV-2 main protease (Mpro) is essential for viral replication and constitutes a promising therapeutic target. Many efforts aimed at deriving effective Mpro inhibitors are currently underway, including an international...
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[NMR paper] Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy.
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy.
Related Articles Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy.
Angew Chem Int Ed Engl. 1999 Jun 14;38(12):1784-1788
Authors: Mayer M, Meyer B
Abstract
Fast identification of binding activity directly from mixtures of potential ligands is possible with the NMR method described, which is based on saturation transfer to molecules in direct contact to a protein. In addition, the ligand's binding epitope is...
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05-03-2018 06:46 PM
[NMR paper] Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Related Articles Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Biochem Biophys Res Commun. 2015 Aug 21;
Authors: Cox BD, Mehta AK, DiRaddo JO, Liotta DC, Wilson LJ, Snyder JP
Abstract
CXCR4 is a GPCR involved in leukocyte trafficking. Small molecule antagonists of the receptor may treat inflammatory disease, cancer and HIV. Here we probe the binding of a...
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08-25-2015 08:30 PM
[NMR paper] NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
Methods Mol Biol. 2014;1200:501-9
Authors: Hemmi H
Abstract
One of the most commonly used...
[NMR paper] Specific RNA-protein interactions detected with saturation transfer difference NMR.
Specific RNA-protein interactions detected with saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.landesbioscience.com-icon-pubmed-Landesbioscience2.jpg Specific RNA-protein interactions detected with saturation transfer difference NMR.
RNA Biol. 2013 Jul 30;10(8)
Authors: Harris KA, Shekhtman A, Agris PF
Abstract
RNA, at the forefront of biochemical research due to its central role in biology, is recognized by proteins through various mechanisms. Analysis of the...
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08-21-2013 08:49 PM
[NMR paper] Monomer-collagen interactions studied by saturation transfer difference NMR.
Monomer-collagen interactions studied by saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-sage.gif Related Articles Monomer-collagen interactions studied by saturation transfer difference NMR.
J Dent Res. 2013 Mar;92(3):284-8
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagami J
Abstract
Functional monomers in dentin adhesives are involved in wetting dental substrates, demineralization, and the formation of calcium salts....
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04-09-2013 06:31 PM
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy
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