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 minimizes possible perturbations in the...
[NMR paper] Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein-Protein and Protein-Ligand Interactions.
Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein-Protein and Protein-Ligand Interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein-Protein and Protein-Ligand Interactions.
J Am Chem Soc. 2021 Jan 05;:
Authors: Abdelkader EH, Qianzhu H, Tan YJ, Adams LA, Huber T, Otting G
Abstract
Trimethylsilyl (TMS)...
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[ASAP] Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein–Protein and Protein–Ligand Interactions
Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein–Protein and Protein–Ligand Interactions
Elwy H. Abdelkader, Haocheng Qianzhu, Yi Jiun Tan, Luke A. Adams, Thomas Huber, and Gottfried Otting
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c11971/20210105/images/medium/ja0c11971_0013.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c11971
http://feeds.feedburner.com/~r/acs/jacsat/~4/IY4qiv61wDE
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01-06-2021 07:11 AM
[NMR paper] Erratum to: Protein-protein interaction analysis in crude bacterial lysates using combinational method of (19)F site-specific incorporation and (19)F NMR.
Erratum to: Protein-protein interaction analysis in crude bacterial lysates using combinational method of (19)F site-specific incorporation and (19)F NMR.
Related Articles Erratum to: Protein-protein interaction analysis in crude bacterial lysates using combinational method of (19)F site-specific incorporation and (19)F NMR.
Protein Cell. 2017 Mar 10;:
Authors: Li D, Zhang Y, He Y, Zhang C, Wang J, Xiong Y, Zhang L, Liu Y, Shi P, Tian C
PMID: 28284007
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03-12-2017 12:32 PM
Bacterial production of site specific 13 C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins
Bacterial production of site specific 13 C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins
Abstract
Nuclear magnetic resonance spectroscopy studies of ever larger systems have benefited from many different forms of isotope labeling, in particular, site specific isotopic labeling. Site specific 13C labeling of methyl groups has become an established means of probing systems not amenable to traditional methodology. However useful, methyl reporter sites can be limited in number and/or...
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12-27-2016 11:04 PM
Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation
From The DNP-NMR Blog:
Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation
This article was already published in 2009 but unfortunately I missed it.
Pavlova, A., et al., Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation. Phys. Chem. Chem. Phys., 2009. 11(31): p. 6833-6839.
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11-21-2013 01:14 AM
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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01-18-2011 10:22 PM
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
Biochemistry. 2011 Jan 12;
Authors: He Y, Estephan R, Yang X, Vela A, Wang H, Bernard C, Stark RE
Liver fatty acid-binding protein (LFABP) is a 14-kDa cytosolic polypeptide, differing from other family members in number of ligand binding sites, diversity of bound ligands, and transfer of fatty acid(s) to...
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01-14-2011 12:05 PM
[NMR paper] NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies
NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
Biochemistry. 1996 Jul 30;35(30):9637-46
Authors: Scheuring J, Fischer M, Cushman M, Lee J, Bacher A,...
Site-Specific Incorporation of 7-Fluoro-L-tryptophan into Proteins by Genetic Encoding to Monitor Ligand Binding by (19)F NMR Spectroscopy
Linear Mode
