The substitution of a single hydrogen atom in a protein by fluorine yields a site-specific probe for sensitive detection by ^(19)F nuclear magnetic resonance (NMR) spectroscopy, where the absence of background signal from the protein facilitates the detection of minor conformational species. We developed genetic encoding systems for the site-selective incorporation of 4-fluorotryptophan, 5-fluorotryptophan, 6-fluorotryptophan, and 7-fluorotryptophan in response to an amber stop codon and used...
[NMR paper] NMR Characterization of the Papain-like Protease from SARS-CoV-2 Identifies the Conformational Heterogeneity in Its Inhibitor-Binding Site
NMR Characterization of the Papain-like Protease from SARS-CoV-2 Identifies the Conformational Heterogeneity in Its Inhibitor-Binding Site
Papain-like protease (PLpro) from severe acute respiratory syndrome Coronavirus 2 (SARS-CoV-2) is a prime target for the development of antivirals for Coronavirus disease 2019 (COVID-19). However, drugs that target the PLpro protein have not yet been approved. In order to gain insights into the development of a PLpro inhibitor, conformational dynamics of PLpro in complex with GRL0617, the most well-characterized PLpro inhibitor, were investigated using...
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07-21-2023 11:16 PM
[NMR paper] Site-Specific Incorporation of 7-Fluoro-L-tryptophan into Proteins by Genetic Encoding to Monitor Ligand Binding by (19)F NMR Spectroscopy
Site-Specific Incorporation of 7-Fluoro-L-tryptophan into Proteins by Genetic Encoding to Monitor Ligand Binding by (19)F NMR Spectroscopy
A mutant aminoacyl-tRNA synthetase identified by a library selection system affords site-specific incorporation of 7-fluoro-L-tryptophan in response to an amber stop codon. The enzyme allows the production of proteins with a single hydrogen atom replaced by a fluorine atom as a sensitive nuclear magnetic resonance (NMR) probe. The substitution of a single hydrogen atom by another element that is as closely similar in size and hydrophobicity as possible...
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01-11-2022 06:11 PM
[NMR paper] Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.
Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.
J Biomol NMR. 2020 Jun 08;:
Authors: Li J, Sae Her A, Traaseth NJ
Abstract
NMR spectroscopy is commonly used to infer site-specific acid dissociation constants (pKa) since the chemical shift is...
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06-11-2020 06:01 PM
Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy
Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy
Abstract
NMR spectroscopy is commonly used to infer site-specific acid dissociation constants (pKa) since the chemical shift is sensitive to the protonation state. Methods that probe atoms nearest to the functional groups involved in acid/base chemistry are the most sensitive for determining the protonation state. In this work, we describe a magic-angle-spinning (MAS) solid-state NMR approach to measure chemical shifts on the side chain of the anionic residues...
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06-08-2020 09:09 PM
[ASAP] Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR
Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR
Nadide Altincekic†‡, Frank Lo¨hr‡§, Jakob Meier-Credo?, Julian D. Langer?, Martin Hengesbach†, Christian Richter†‡, and Harald Schwalbe*†‡
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c02308/20200414/images/medium/ja0c02308_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c02308
http://feeds.feedburner.com/~r/acs/jacsat/~4/do84CXaCia8
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[NMR paper] Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.
Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.
J Am Chem Soc. 2020 Apr 01;:
Authors: Altincekic N, L?hr F, Meier-Credo J, Langer JD, Hengesbach M, Richter C, Schwalbe H
Abstract
Post-translational modifications of...
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04-03-2020 09:41 PM
[NMR paper] Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13140-3
Authors: Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA
Abstract
At the...
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06-12-2013 11:42 AM
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Biophys J. 2011 Aug 3;101(3):L23-L25
Authors: Wang S, Shi L, Kawamura I, Brown LS, Ladizhansky V
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific...
Genetic Encoding of Fluoro-l-tryptophans for Site-Specific Detection of Conformational Heterogeneity in Proteins by NMR Spectroscopy
Linear Mode
