O - Tert -Butyltyrosine, an NMR Tag for High-Molecular-Weight Systems and Measurements of Submicromolar Ligand Binding Affinities

Journal of the American Chemical Society

Volumn 137, Issue 13, 2015, Pages 4581-4586

  Chen, Wan Na ^a   Kuppan, Kekini Vahini ^a   Lee, Michael David ^b   Jaudzems, Kristaps ^c   Huber, Thomas ^a   Otting, Gottfried ^a  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

^b MONASH UNIVERSITY   (Australia)

^c LATVIAN INSTITUTE OF ORGANIC SYNTHESIS   (Latvia)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; BINDING ENERGY; DISSOCIATION; ESCHERICHIA COLI; ISOMERS; ISOTOPES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; RESONANCE;

BACILLUS STEAROTHERMOPHILUS; CHEMICAL EQUIVALENCE; DISSOCIATION CONSTANT; HIGH MOLECULAR WEIGHT; LIGAND BINDING AFFINITY; PROTEIN DETECTION; QUANTITATIVE MEASUREMENT; UNNATURAL AMINO ACIDS;

NUCLEAR MAGNETIC RESONANCE;

ASPARTIC ACID; BINDING PROTEIN; DIMETHYL SULFOXIDE; GLUTAMIC ACID; O TERT BUTYLTYROSINE; PROTON; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG; 3'-TERT-BUTYLTYROSINE; DNAB HELICASE; LIGAND; TYROSINE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CALCIUM BINDING; CELL FREE SYSTEM; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; DIPOLE; DISSOCIATION CONSTANT; ESCHERICHIA COLI; FLUORINE NUCLEAR MAGNETIC RESONANCE; GEOBACILLUS STEAROTHERMOPHILUS; ISOTOPE LABELING; LIGAND BINDING; MOLECULAR WEIGHT; NONHUMAN; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE ANALYSIS; REMOTE SENSING; STAPHYLOCOCCUS AUREUS; SUBMICROMOLAR LIGAND BINDING AFFINITY; WILD TYPE; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; ENZYMOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE;

DNAB HELICASES; ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS; ISOTOPE LABELING; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR WEIGHT; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; TYROSINE;

EID: 84926662602     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/jacs.5b01918     Document Type: Article

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