Related ArticlesSolid-state NMR: An emerging technique in structural biology of self-assemblies.
Biophys Chem. 2015 Jul 16;
Authors: Habenstein B, Loquet A
Abstract
Protein self-assemblies are ubiquitous biological systems involved in many cellular processes, ranging from bacterial and viral infection to the propagation of neurodegenerative disorders. Studying the atomic three-dimensional structures of protein self-assemblies is a particularly demanding task, as these systems are usually insoluble, non-crystalline and of large size. Solid-state NMR (ssNMR) is an emerging method that can provide atomic-level structural data on intact macromolecular assemblies. We here present recent progress in magic-angle spinning ssNMR to study protein assemblies and give an overview on its combination with complementary techniques such as cryo-EM, mass-per-length measurements, SAXS and X-ray diffraction. Applications of ssNMR on its own and in hybrid approaches have revealed precious atomic details and first high-resolution structures of complex biological assemblies, including amyloid fibrils, bacterial filaments, phages or virus capsids.
PMID: 26234527 [PubMed - as supplied by publisher]
Magic Angle Spinning NMR Spectroscopy: A Versatile Technique for Structural and Dynamic Analysis of Solid-Phase Systems
From The DNP-NMR Blog:
Magic Angle Spinning NMR Spectroscopy: A Versatile Technique for Structural and Dynamic Analysis of Solid-Phase Systems
This review gives a comprehensive overview of the state-of-the-art of magic-angle spinning (MAS), solid-state NMR spectroscopy, including DNP-NMR spectroscopy.
1. Polenova, T., R. Gupta, and A. Goldbourt, Magic angle spinning NMR spectroscopy: a versatile technique for structural and dynamic analysis of solid-phase systems. Anal Chem, 2015. 87(11): p. 5458-69.
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06-29-2015 07:21 PM
[NMR paper] Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes.
Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes.
Related Articles Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes.
J Magn Reson. 2014 Nov 15;
Authors: Fricke P, Chevelkov V, Shi C, Lange A
Abstract
Solid-state NMR is a versatile tool to study structure and dynamics of insoluble and non-crystalline biopolymers. Supramolecular protein assemblies are formed by self-association of multiple copies of single small-sized...
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12-10-2014 06:29 PM
[NMR paper] Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes
Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes
Publication date: Available online 15 November 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Pascal Fricke , Veniamin Chevelkov , Chaowei Shi , Adam Lange</br>
Solid-state NMR is a versatile tool to study structure and dynamics of insoluble and non-crystalline biopolymers. Supramolecular protein assemblies are formed by self-association of multiple copies of single small-sized proteins. Because of their high degree of local order, solid-state NMR...
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11-16-2014 02:13 AM
Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology
From The DNP-NMR Blog:
Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology
Gelis, I., et al., Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology. J. Biomol. NMR, 2013. 56(2): p. 85-93.
http://dx.doi.org/10.1007/s10858-013-9721-2
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09-09-2013 05:14 PM
Cu-SOD structure and dynamics by solid-state NMR [Biophysics and Computational Biology]
Cu-SOD structure and dynamics by solid-state NMR
Knight, M. J., Pell, A. J., Bertini, I., Felli, I. C., Gonnelli, L., Pierattelli, R., Herrmann, T., Emsley, L., Pintacuda, G....
Date: 2012-07-10
We introduce a new approach to improve structural and dynamical determination of large metalloproteins using solid-state nuclear magnetic resonance (NMR) with 1H detection under ultrafast magic angle spinning (MAS). The approach is based on the rapid and sensitive acquisition of an extensive set of 15N and 13C nuclear relaxation rates. The system on which we demonstrate these methods is the...
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07-10-2012 06:01 PM
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method [Biophysics and Computational Biology]
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
Verardi, R., Shi, L., Traaseth, N. J., Walsh, N., Veglia, G....
Date: 2011-05-31
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca2+-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and...
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05-31-2011 11:41 PM
(13)C Spin Dilution for Simplified and Complete Solid-State NMR Resonance Assignment of Insoluble Biological Assemblies.
(13)C Spin Dilution for Simplified and Complete Solid-State NMR Resonance Assignment of Insoluble Biological Assemblies.
(13)C Spin Dilution for Simplified and Complete Solid-State NMR Resonance Assignment of Insoluble Biological Assemblies.
J Am Chem Soc. 2011 Mar 14;
Authors: Loquet A, Lv G, Giller K, Becker S, Lange A
A strategy for simplified and complete resonance assignment of insoluble and noncrystalline proteins by solid-state NMR (ssNMR) spectroscopy is presented. Proteins produced with - or glucose are very sparsely labeled, and the...
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03-16-2011 04:15 PM
13C Spin Dilution for Simplified and Complete Solid-State NMR Resonance Assignment of Insoluble Biological Assemblies
13C Spin Dilution for Simplified and Complete Solid-State NMR Resonance Assignment of Insoluble Biological Assemblies
Antoine Loquet, Guohua Lv, Karin Giller, Stefan Becker and Adam Lange
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja200066s/aop/images/medium/ja-2011-00066s_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja200066s
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/aFxzgJtJWtI