Výsledky vyhledávání - "Haocheng Qianzhu"

Through-Space Scalar 19F–19F Couplings between Fluorinated Noncanonical Amino Acids for the Detection of Specific Contacts in Proteins

Autor: Henry W. Orton, Elwy H. Abdelkader, Rebecca L. Frkic, Edan I Habel, Colin J. Jackson, Haocheng Qianzhu, Yi Jiun Tan, Gottfried Otting, Thomas Huber

Publikováno v: Journal of the American Chemical Society. 143:19587-19598

Fluorine atoms are known to display scalar 19F-19F couplings in nuclear magnetic resonance (NMR) spectra when they are sufficiently close in space for nonbonding orbitals to overlap. We show that fluorinated noncanonical amino acids positioned in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::537edd439a3a933be41288d175a872fe
https://doi.org/10.1021/jacs.1c10104

Zobrazit plný text záznamu

Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein–Protein and Protein–Ligand Interactions

Autor: Gottfried Otting, Elwy H. Abdelkader, Thomas Huber, Yi Jiun Tan, Haocheng Qianzhu, Luke A. Adams

Publikováno v: Journal of the American Chemical Society. 143:1133-1143

Trimethylsilyl (TMS) groups present outstanding NMR probes of biological macromolecules as they produce intense singlets in 1H NMR spectra near 0 ppm, where few other proton resonances occur. We report a system for genetic encoding of N6-(((trimethyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f808972a8809c260d6f4d4511fd89589
https://doi.org/10.1021/jacs.0c11971

Zobrazit plný text záznamu

Genetic Encoding of para-Pentafluorosulfanyl Phenylalanine: A Highly Hydrophobic and Strongly Electronegative Group for Stable Protein Interactions

Autor: Gottfried Otting, Adarshi P. Welegedara, Haocheng Qianzhu, Mithun C. Mahawaththa, Nicholas E. Dixon, Amy E. McGrath, Thomas Huber, Holly Williamson

Publikováno v: Journal of the American Chemical Society. 142:17277-17281

SF5Phe, para-pentafluorosulfanyl phenylalanine, is an unnatural amino acid with extreme physicochemical properties, which is stable in physiological conditions. Here we present newly developed aminoacyl-tRNA synthetases that enable genetic encoding o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2a754766a97b2a6952213f950eab94dc
https://doi.org/10.1021/jacs.0c07976

Zobrazit plný text záznamu

Site-Specific Incorporation of 7-Fluoro-L-tryptophan into Proteins by Genetic Encoding to Monitor Ligand Binding by

Autor: Haocheng, Qianzhu, Elwy H, Abdelkader, Iresha D, Herath, Gottfried, Otting, Thomas, Huber

Publikováno v: ACS sensors. 7(1)

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 repl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cadd1035f3a2a45d2d98335d8255f64b
https://pubmed.ncbi.nlm.nih.gov/35005899

Zobrazit plný text záznamu

Genetic Encoding of Cyanopyridylalanine for In-Cell Protein Macrocyclization by the Nitrile-Aminothiol Click Reaction

Autor: Rebecca L. Frkic, Haocheng Qianzhu, Josemon George, Elwy H. Abdelkader, Christoph Nitsche, Gottfried Otting, Colin J. Jackson, Thomas Huber

Publikováno v: Angewandte Chemie (International ed. in English). 61(13)

Cyanopyridylalanines are non-canonical amino acids that react with aminothiol compounds under physiological conditions in a biocompatible manner without requiring added catalyst. Here we present newly developed aminoacyl-tRNA synthetases for genetic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ee3083cae99bf4ae9f4761be9d46060
https://pubmed.ncbi.nlm.nih.gov/35102680

Zobrazit plný text záznamu

Genetic Encoding of

Autor: Elwy H, Abdelkader, Haocheng, Qianzhu, Yi Jiun, Tan, Luke A, Adams, Thomas, Huber, Gottfried, Otting

Publikováno v: Journal of the American Chemical Society. 143(2)

Trimethylsilyl (TMS) groups present outstanding NMR probes of biological macromolecules as they produce intense singlets in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a8c377980b33f89c4e3876041cd86c03
https://pubmed.ncbi.nlm.nih.gov/33399460

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání