Abstract:
:To elucidate the structures and dynamics of membrane proteins, highly advanced biophysical methods have been developed that often require significant resources, both for sample preparation and experimental analyses. For very complex systems, such as membrane transporters, ion channels or G-protein coupled receptors (GPCRs), the incorporation of a single reporter at a select site can significantly simplify the observables and the measurement/analysis requirements. Here we present examples using 19F nuclear magnetic resonance (NMR) spectroscopy as a powerful, yet relatively straightforward tool to study (membrane) protein structure, dynamics and ligand interactions. We summarize methods to incorporate 19F labels into proteins and discuss the type of information that can be readily obtained for membrane proteins already from relatively simple NMR spectra with a focus on GPCRs as the membrane protein family most extensively studied by this technique. In the future, these approaches may be of particular interest also for many proteins that undergo complex functional dynamics and/or contain unstructured regions and thus are not amenable to X-ray crystallography or cryo electron microscopy (cryoEM) studies.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Rose-Sperling D,Tran MA,Lauth LM,Goretzki B,Hellmich UAdoi
10.1515/hsz-2018-0473subject
Has Abstractpub_date
2019-09-25 00:00:00pages
1277-1288issue
10eissn
1431-6730issn
1437-4315pii
/j/bchm.just-accepted/hsz-2018-0473/hsz-2018-0473.journal_volume
400pub_type
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