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 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 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 studies.
PMID: 31004560 [PubMed - as supplied by publisher]
[NMR paper] NMR as a tool to investigate the structure, dynamics and function of membrane proteins.
NMR as a tool to investigate the structure, dynamics and function of membrane proteins.
NMR as a tool to investigate the structure, dynamics and function of membrane proteins.
Nat Struct Mol Biol. 2016 Jun 7;23(6):468-474
Authors: Liang B, Tamm LK
Abstract
Membrane-protein NMR occupies a unique niche for determining structures, assessing dynamics, examining folding, and studying the binding of lipids, ligands and drugs to membrane proteins. However, NMR analyses of membrane proteins also face special challenges that are not...
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06-09-2016 07:44 PM
Improvements to REDCRAFT: a software tool for simultaneous characterization of protein backbone structure and dynamics from residual dipolar couplings
Improvements to REDCRAFT: a software tool for simultaneous characterization of protein backbone structure and dynamics from residual dipolar couplings
Abstract
Within the past two decades, there has been an increase in the acquisition of residual dipolar couplings (RDC) for investigations of biomolecular structures. Their use however is still not as widely adopted as the traditional methods of structure determination by NMR, despite their potential for extending the limits in studies that examine both the structure and dynamics of biomolecules. This...
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11-17-2014 12:48 PM
[NMR900 blog] New book: NMR Spectroscopy: A Versatile Tool for Environmental Research
New book: NMR Spectroscopy: A Versatile Tool for Environmental Research
Myrna J. Simpson (Editor)
Andre J. Simpson (Editor)
Hardcover: 448 pages
Publisher: Wiley; July 2014
Language: English
ISBN: 978-1118616475
http://ca.wiley.com/WileyCDA/WileyTitle/productCd-1118616472.html
http://www.amazon.com/dp/1118616472
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06-30-2014 07:33 AM
New Tool for Studying Membrane Protein Structure - Science Daily (press release)
New Tool for Studying Membrane Protein Structure - Science Daily (press release)
<img alt="" height="1" width="1" />
New Tool for Studying Membrane Protein Structure
Science Daily (press release)
The team used Overhauser dynamic nuclear polarization enhanced nuclear magnetic resonance (NMR), a technique they developed over the last few years. Using a small and stable radical with an even higher magnetic property than the hydrogen atom of ...
Read here
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10-03-2013 02:41 AM
New Tool for Studying Membrane Protein Structure - Science Daily (press release)
<img alt="" height="1" width="1" />
New Tool for Studying Membrane Protein Structure
Science Daily (press release)
The team used Overhauser dynamic nuclear polarization enhanced nuclear magnetic resonance (NMR), a technique they developed over the last few years. Using a small and stable radical with an even higher magnetic property than the hydrogen atom of ...
and more »
New Tool for Studying Membrane Protein Structure - Science Daily (press release)
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10-01-2013 11:15 PM
[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
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11-24-2010 11:14 PM
[NMR paper] Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculatio
Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation.
J Magn Reson. 1997 Jan;124(1):154-64
Authors: Stein EG, Rice LM, BrĂ¼nger AT
Molecular dynamics in torsion-angle space was applied to nuclear magnetic resonance structure calculation using nuclear Overhauser effect-derived distances and...
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08-22-2010 03:03 PM
Simultaneous Structure and Dynamics of a Membrane Protein using REDCRAFT: Membrane-bo
Simultaneous Structure and Dynamics of a Membrane Protein using REDCRAFT: Membrane-bound form of Pf1 Coat Protein
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 30 July 2010</br>
Paul, Shealy , Mikhail, Simin , Sang Ho, Park , Stanley J., Opella , Homayoun, Valafar</br>
A strategy for simultaneous study of the structure and internal dynamics of a membrane protein is described using the REDCRAFT algorithm. The membrane-bound form of the Pf1 major coat protein (mbPf1) was used as an example. First, synthetic data is...