Using (19)F NMR to probe biological interactions of proteins and peptides

Fluorine is a valuable probe for investigating the interactions of biological molecules because of its favorable NMR characteristics, its small size, and its near total absence from biology. Advances in biosynthetic methods allow fluorine to be introduced into peptides and proteins with high precisi...

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Bibliographic Details
Published in:ACS chemical biology 2014-06, Vol.9 (6), p.1242-1250
Main Authors: Marsh, E Neil G, Suzuki, Yuta
Format: Article
Language:English
Subjects:
Animals
Fluorine - chemistry
Humans
Nuclear Magnetic Resonance, Biomolecular - methods
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Proteins - chemistry
Proteins - metabolism
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Summary:Fluorine is a valuable probe for investigating the interactions of biological molecules because of its favorable NMR characteristics, its small size, and its near total absence from biology. Advances in biosynthetic methods allow fluorine to be introduced into peptides and proteins with high precision, and the increasing sensitivity of NMR spectrometers has facilitated the use of (19)F NMR to obtain molecular-level insights into a wide range of often-complex biological interactions. Here, we summarize the advantages of solution-state (19)F NMR for studying the interactions of peptides and proteins with other biological molecules, review methods for the production of fluorine-labeled materials, and describe some representative recent examples in which (19)F NMR has been used to study conformational changes in peptides and proteins and their interactions with other biological molecules.
ISSN:1554-8937
DOI:10.1021/cb500111u