Lanthanoid tagging via an unnatural amino acid for protein structure characterization
Lanthanoid tagging via an unnatural amino acid for protein structure characterization
Abstract
Lanthanoid pseudo-contact shift (PCS) provides long-range structural information between a paramagnetic tag and protein nuclei. However, for proteins with native cysteines, site-specific attachment may only utilize functional groups orthogonal to sulfhydryl chemistry. Here we report two lanthanoid probes, DTTA-C3-yne and DTTA-C4-yne, which can be conjugated to an unnatural amino acid pAzF in the target protein via azide-alkyne cycloaddition. Demonstrated...
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04-01-2017 04:09 PM
[NMR paper] Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Related Articles Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Org Biomol Chem. 2017 Jan 27;:
Authors: Lv C, Feng L, Zhao H, Wang G, Stavropoulos P, Ai L
Abstract
In the field of chiral recognition, reported chiral discrimination by (1)H NMR spectroscopy has mainly focused on...
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01-28-2017 08:29 PM
Incorporation of an Unnatural Amino Acid as a Domain-SpecificFluorescence Probe in a Two-Domain Protein
Incorporation of an Unnatural Amino Acid as a Domain-SpecificFluorescence Probe in a Two-Domain Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00898/20161129/images/medium/bi-2016-00898m_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00898
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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11-29-2016 09:02 PM
[NMR paper] The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.
The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.
Biopolymers. 2013 Aug;99(8):548-61
Authors: Clark TD,...
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04-23-2016 09:24 PM
[NMR paper] Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Nat Commun. 2015;6:8202
Authors: Yang F, Yu X, Liu C, Qu CX, Gong Z, Liu HD, Li FH, Wang HM, He DF, Yi F, Song C, Tian CL, Xiao KH, Wang JY, Sun JP
Abstract
Specific arrestin conformations are coupled to distinct downstream effectors, which underlie the functions of many...
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09-09-2015 11:49 AM
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Abstract
The use of paramagnetic constraints in protein NMR is an active area of research because of the benefits of long-range distance measurements (>10Â*Ã?). One of the main issues in successful execution is the incorporation of a paramagnetic metal ion into diamagnetic proteins. The most common metal ion tags are relatively long aliphatic chains attached to the side chain of a...
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11-28-2014 11:37 AM
An efficient protocol for incorporation of an unnatural amino acid in perdeuterated recombinant proteins using glucose-based media
An efficient protocol for incorporation of an unnatural amino acid in perdeuterated recombinant proteins using glucose-based media
Abstract The in vivo incorporation of unnatural amino acids into proteins is a well-established technique requiring an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is incorporated at a position encoded by a TAG amber codon. Although this technology provides unique opportunities to engineer protein structures, poor protein yields are usually obtained in deuterated media, hampering its application in the protein NMR...
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02-21-2012 03:40 AM
Site-specific labeling of proteins with NMR-active unnatural amino acids
Site-specific labeling of proteins with NMR-active unnatural amino acids
Abstract A large number of amino acids other than the canonical amino acids can now be easily incorporated in vivo into proteins at genetically encoded positions. The technology requires an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is added to the media while a TAG amber or frame shift codon specifies the incorporation site in the protein to be studied. These unnatural amino acids can be isotopically labeled and provide unique opportunities for site-specific labeling...
Computational protein design utilizes unnatural amino acids - Phys.Org
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