Publication date: Available online 15 November 2014 Source:Journal of Magnetic Resonance
Author(s): Pascal Fricke , Veniamin Chevelkov , Chaowei Shi , Adam Lange
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 spectra of such systems exhibit an unusually high level of resolution, rendering them an ideal target for solid-state NMR investigations. Recently, our group has solved the structure of one particular supramolecular assembly, the type-iii-secretion-system needle. The needle subunit comprises around 80 residues. Many interesting supramolecular assemblies with unknown structure have subunits larger in size, which requires development of tailored solid-state NMR strategies to address their structures. In this “Perspective” article, we provide a view on different approaches to enhance sensitivity and resolution in biological solid-state NMR with a focus on the possible application to supramolecular assemblies with large subunit sizes. Graphical abstract
[NMR paper] Solid-State NMR-Based Approaches for Supramolecular Structure Elucidation.
Solid-State NMR-Based Approaches for Supramolecular Structure Elucidation.
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Acc Chem Res. 2013 Apr 15;
Authors: Weingarth M, Baldus M
Abstract
Supramolecular chemistry provides structural and conformational information about complexes formed from multiple molecules. While the molecule is held together by strong intramolecular contacts like covalent bonds, supramolecular structures can be further stabilized by weaker or transient intermolecular...
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04-17-2013 08:15 PM
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
Abstract Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance assignment of methyl probes in high molecular weight protein assemblies can be efficiently achieved by combining fast NMR experiments, residue-type-specific isotope-labeling and automated site-directed mutagenesis. The utility of this general and straightforward strategy is demonstrated through...
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06-06-2011 12:53 AM
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
J Biomol NMR. 2011 May 29;
Authors: Amero C, Asunción Durá M, Noirclerc-Savoye M, Perollier A, Gallet B, Plevin MJ, Vernet T, Franzetti B, Boisbouvier J
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance...
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06-01-2011 02:30 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
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03-15-2011 05:56 AM
[NMR paper] TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution.
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Trends Biochem Sci. 2000 Oct;25(10):462-8
Authors: Riek R, Pervushin K, Wüthrich K
TROSY and CRINEPT are new techniques for solution NMR studies of molecular and supramolecular structures. They allow the collection of high-resolution spectra of structures with molecular weights >100 kDa, significantly extending the range of macromolecular systems that can...
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11-19-2010 08:29 PM
Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy.
Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy.
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J Am Chem Soc. 2010 Oct 8;
Authors: Loquet A, Giller K, Becker S, Lange A
We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein-protein complexes. The method relies on the measurement of intermolecular (13)C-(13)C distances in mixtures of glucose- and glucose-labeled proteins. We have...
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10-12-2010 02:52 PM
Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy
Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy
Antoine Loquet, Karin Giller, Stefan Becker and Adam Lange
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107460j/aop/images/medium/ja-2010-07460j_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107460j
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