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• W2024882722 startingPage "2054" @default.
• W2024882722 abstract "Solution NMR studies of protein structure and dynamics using fluorinated amino acid probes are a valuable addition to the repertoire of existing (13)C, (15)N, and (1)H experiments. Despite the numerous advantages of the (19)F nucleus in NMR, protein studies are complicated by the dependence of resonance assignments on site-directed mutagenesis methods which are laborious and often problematic. Here we report an NMR-based route to the assignment of fluorine resonances in (13)C,(15)N-3-fluoro-l-tyrosine labeled calmodulin. The assignment begins with the correlation of the fluorine nucleus to the delta proton in the novel (13)C,(15)N-enriched probe which is achieved using a CT-HCCF-COSY experiment. Connection to the backbone is made through two additional solution NMR experiments, namely the (H(beta))C(beta)(C(gamma)C(delta))H(delta) and HNCACB. Assignments are completed using either previously published backbone chemical shift data or obtained experimentally provided uniform (13)C,(15)N labeling procedures are employed during protein expression. Additional benefits of the (13)C,(15)N-3-fluoro-l-tyrosine probe include the reduction of spectral overlap through ((13)C(19)F) CT-HSQCs, as well as the ability to monitor side chain dynamics using (19)F T(1), T(2), and the (13)C-(19)F NOE." @default.
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• W2024882722 date "2009-01-27" @default.
• W2024882722 modified "2023-10-18" @default.
• W2024882722 title "A Mutagenesis-Free Approach to Assignment of ¹⁹F NMR Resonances in Biosynthetically Labeled Proteins" @default.
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• W2024882722 doi "https://doi.org/10.1021/ja8085752" @default.
• W2024882722 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19173647" @default.
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