Fucosylation patterns in cell-surface glycans are essential mediators of recognition and signalling. Aberrations in these signatures serve as vital diagnostic markers of disease progression, and so understanding fucose-protein interactions at the molecular level is crucial. Molecular editing of l-fucose (Fuc) at C2 with fluorine provides a platform to reconcile the ubiquity of fucosylation with the paucity of strategies to interrogate site-specific interactions. Through judicious introduction of...
[NMR paper] Genetic Encoding of Fluoro-l-tryptophans for Site-Specific Detection of Conformational Heterogeneity in Proteins by NMR Spectroscopy
Genetic Encoding of Fluoro-l-tryptophans for Site-Specific Detection of Conformational Heterogeneity in Proteins by NMR Spectroscopy
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...
[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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[NMR paper] Interrogation of solution conformation of complex macrocyclic peptides utilizing a combined SEC-HDX-MS, circular dichroism, and NMR workflow
Interrogation of solution conformation of complex macrocyclic peptides utilizing a combined SEC-HDX-MS, circular dichroism, and NMR workflow
Recent technological and synthetic advances have led to a resurgence in the exploration of peptides as potential therapeutics. Understanding peptide conformation in both free and protein-bound states remains one of the most critical areas for successful development of peptide drugs. In this study it was demonstrated that the combination of Size-Exclusion Chromatography with Hydrogen-Deuterium Exchange Mass Spectrometry (SEC-HDX-MS) and Circular...
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The Cation-? Interaction Enables a Halo-TagFluorogenic Probe for Fast No-Wash Live Cell Imaging and Gel-FreeProtein Quantification
The Cation-? Interaction Enables a Halo-TagFluorogenic Probe for Fast No-Wash Live Cell Imaging and Gel-FreeProtein Quantification
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00056/20170308/images/medium/bi-2017-00056j_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00056
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[NMR paper] Vitamin C metabolomic mapping in the lens with 6-deoxy-6-fluoro-ascorbic acid and hig
Vitamin C metabolomic mapping in the lens with 6-deoxy-6-fluoro-ascorbic acid and high-resolution 19F-NMR spectroscopy.
Related Articles Vitamin C metabolomic mapping in the lens with 6-deoxy-6-fluoro-ascorbic acid and high-resolution 19F-NMR spectroscopy.
Invest Ophthalmol Vis Sci. 2003 May;44(5):2047-58
Authors: Satake M, Dmochowska B, Nishikawa Y, Madaj J, Xue J, Guo Z, Reddy DV, Rinaldi PL, Monnier VM
PURPOSE: Metabolomics, or metabolic profiling, is an emerging discipline geared to providing information on a large number of metabolites,...
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11-24-2010 09:01 PM
[NMR paper] 19F NMR studies on 8-fluoroflavins and 8-fluoro flavoproteins.
19F NMR studies on 8-fluoroflavins and 8-fluoro flavoproteins.
Related Articles 19F NMR studies on 8-fluoroflavins and 8-fluoro flavoproteins.
Biochemistry. 1990 Mar 20;29(11):2670-9
Authors: Macheroux P, Kojiro CL, Schopfer LM, Chakraborty S, Massey V
The 19F NMR spectra of the oxidized and reduced forms of 8-fluororiboflavin, 8-fluoro-FAD, and the 8-fluoroflavin-reconstituted flavoproteins flavodoxin, riboflavin binding protein, D-amino acid oxidase, p-hydroxybenzoate hydroxylase, Old Yellow Enzyme, anthranilate hydroxylase, general acyl-CoA...
Fluoro-Fucosylation Enables the Interrogation of the Lea - LecB Interaction by BioNMR Spectroscopy
Linear Mode
