Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Edward J Koleski"'
Autor:
Matthew A. Davis, Vivian Yaci Yu, Beverly Fu, Miao Wen, Edward J. Koleski, Joshua Silverman, Charles A. Berdan, Daniel K. Nomura, Michelle C. Y. Chang
Living organisms carry out a wide range of remarkable functions, including the synthesis of thousands of simple and complex chemical structures for cellular growth and maintenance. The manipulation of this reaction network has allowed for the genetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2af3a115deac6a58ac575e8f0cd073a4
https://doi.org/10.1101/2023.01.09.523327
https://doi.org/10.1101/2023.01.09.523327
Autor:
Paul J. Dauenhauer, Edward J Koleski, Zhen Q. Wang, Heng Song, Michelle C. Y. Chang, Dae Sung Park, Yejin Min, Gaurav Kumar, Noritaka Hara
Publikováno v:
Nature Chemistry. 13:1178-1185
Living systems provide a promising approach to chemical synthesis, having been optimized by evolution to convert renewable carbon sources, such as glucose, into an enormous range of small molecules. However, a large number of synthetic structures can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8639ad006f30801e4ebd411605cc70e
https://doi.org/10.1038/s41557-021-00820-0
https://doi.org/10.1038/s41557-021-00820-0
Autor:
Keith E. Arntson, Rachel Lynn Staebell, William C. K. Pomerantz, Clifford T. Gee, Edward J. Koleski
Publikováno v:
ChemBioChem. 19:963-969
Protein-Observed Fluorine NMR (PrOF NMR) spectroscopy is an emerging technique for screening and characterizing small-molecule-protein interactions. The choice of which amino acid to label for PrOF NMR can be critical for analysis. Here we report the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9b5a0f7d9e3d19a31e36a7ffc861bcf1
https://doi.org/10.1002/cbic.201700686
https://doi.org/10.1002/cbic.201700686
Autor:
Clifford T, Gee, Keith E, Arntson, Edward J, Koleski, Rachel Lynn, Staebell, William C K, Pomerantz
Publikováno v:
Chembiochem : a European journal of chemical biology. 19(9)
Protein-Observed Fluorine NMR Spectroscopy (PrOF NMR) is an emerging technique for screening and characterizing small molecule-protein interactions. The choice of which amino acid to label for PrOF NMR can be critical for analysis. Here we report the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8f80be9afc507bbd2e900e932dc772ca
https://pubmed.ncbi.nlm.nih.gov/29430847
https://pubmed.ncbi.nlm.nih.gov/29430847
Publikováno v:
Angewandte Chemie International Edition. 54:3735-3739
(19)F NMR spectroscopy of labeled proteins is a sensitive method for characterizing structure, conformational dynamics, higher-order assembly, and ligand binding. Fluorination of aromatic side chains has been suggested as a labeling strategy for smal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a450e7e41859d382f4e6bb933a2fc25
https://doi.org/10.1002/anie.201411658
https://doi.org/10.1002/anie.201411658