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Laser-Initiated Radical Trifluoromethylation of Peptides and Proteins: Application to Mass-Spectrometry-Based Protein Footprinting.


ABSTRACT: Described is a novel, laser-initiated radical trifluoromethylation for protein footprinting and its broad residue coverage. . CF3 reacts with 18 of the 20 common amino acids, including Gly, Ala, Ser, Thr, Asp, and Glu, which are relatively silent with regard to . OH. This new approach to footprinting is a bridge between trifluoromethylation in materials and medicinal chemistry and structural biology and biotechnology. Its application to a membrane protein and to myoglobin show that the approach is sensitive to protein conformational change and solvent accessibility.

SUBMITTER: Cheng M 

PROVIDER: S-EPMC5663992 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Laser-Initiated Radical Trifluoromethylation of Peptides and Proteins: Application to Mass-Spectrometry-Based Protein Footprinting.

Cheng Ming M   Zhang Bojie B   Cui Weidong W   Gross Michael L ML  

Angewandte Chemie (International ed. in English) 20171005 45


Described is a novel, laser-initiated radical trifluoromethylation for protein footprinting and its broad residue coverage. <sup>.</sup> CF<sub>3</sub> reacts with 18 of the 20 common amino acids, including Gly, Ala, Ser, Thr, Asp, and Glu, which are relatively silent with regard to <sup>.</sup> OH. This new approach to footprinting is a bridge between trifluoromethylation in materials and medicinal chemistry and structural biology and biotechnology. Its application to a membrane protein and to  ...[more]

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