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Verhoork, SJM, Killoran, PM and Coxon, CR (2018) Fluorinated Prolines as Conformational Tools and Reporters for Peptide and Protein Chemistry. Biochemistry, 57 (43). pp. 6132-6143. ISSN 1520-4995
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Fluorinated Prolines as Conformational Tools and Reporters for Peptide and Protein Chemistry.pdf - Accepted Version Download (1MB) | Preview |
Abstract
Amide bonds at the proline nitrogen are particularly susceptible to rotation, affording cis and trans isomers. Installation of a stereochemically defined electron-withdrawing fluorine atom or fluorinated groups has the power to influence the cis–trans conformational preferences of the amide bond in X–(F)Pro (where X = any other amino acid). Advantageously, this also provides a sensitive reporter for 19F nuclear magnetic resonance (NMR) studies of protein conformation, interactions, and dynamics. We deliberately use the term “fluorinated prolines” as an all-encompassing term to describe proline analogues containing one or more fluorine atoms and to avoid confusion with the more well-known 4-fluoroprolines. This review presents a critical discussion of the growing repertoire of fluorinated prolines that have been described and, importantly, provides a comparison of their uses and relative influence on amide-bond conformation and discusses the significant potential of using 19F NMR as a tool to probe conformational changes in polypeptides.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | 0601 Biochemistry and Cell Biology, 1101 Medical Biochemistry and Metabolomics, 0304 Medicinal and Biomolecular Chemistry |
| Subjects: | Q Science > QD Chemistry R Medicine > RM Therapeutics. Pharmacology |
| Divisions: | Pharmacy & Biomolecular Sciences |
| Publisher: | American Chemical Society |
| Related URLs: | |
| Date Deposited: | 16 Jan 2019 12:52 |
| Last Modified: | 04 Sep 2021 09:48 |
| DOI or ID number: | 10.1021/acs.biochem.8b00787 |
| URI: | https://researchonline.ljmu.ac.uk/id/eprint/9950 |
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