Bacterial secretion systems are built up from proteins with different physicochemical characteristics, such as highly hydrophobic transmembrane polypeptides, and soluble periplasmic or intracellular domains. A single complex can be composed of more than ten proteins with distinct features, spreading through different cellular compartments. The membrane and multicompartment nature of the proteins, and their large molecular weight make their study challenging. However, information on their...
[NMR paper] Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100*kHz.
Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100*kHz.
Related Articles Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100*kHz.
Solid State Nucl Magn Reson. 2017 Jul 03;:
Authors: Struppe J, Quinn CM, Lu M, Wang M, Hou G, Lu X, Kraus J, Andreas LB, Stanek J, Lalli D, Lesage A, Pintacuda G, Maas W, Gronenborn AM, Polenova T
Abstract
The recent breakthroughs in NMR...
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Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100*kHz
Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100*kHz
Publication date: Available online 3 July 2017
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Jochem Struppe, Caitlin M. Quinn, Manman Lu, Mingzhang Wang, Guangjin Hou, Xingyu Lu, Jodi Kraus, Loren B. Andreas, Jan Stanek, Daniela Lalli, Anne Lesage, Guido Pintacuda, Werner Maas, Angela M. Gronenborn, Tatyana Polenova</br>
The recent breakthroughs in NMR probe technologies resulted in...
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[NMR paper] Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.
Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.
Related Articles Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.
Sci Rep. 2017 Mar 17;7:44506
Authors: Yehl J, Kudryashova E, Reisler E, Kudryashov D, Polenova T
Abstract
Cellular actin dynamics is an essential element of numerous cellular processes, such as cell motility, cell division and...
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03-19-2017 10:38 PM
[NMR paper] Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.
Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.
Related Articles Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.
Q Rev Biophys. 2017 Jan;50:e1
Authors: Quinn CM, Polenova T
Abstract
In recent years, exciting developments in instrument technology and experimental methodology have advanced the field of magic-angle spinning (MAS) nuclear magnetic resonance (NMR) to new heights. Contemporary MAS NMR yields atomic-level insights into structure and...
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01-19-2017 08:56 AM
Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies #DNPNMR
Gupta, R., et al., Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies. J Phys Chem B, 2016. 120(2): p. 329-39.
http://www.ncbi.nlm.nih.gov/pubmed/26709853
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[NMR paper] The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography.
The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography.
Chembiochem. 2015 May...
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[NMR paper] Dynamic Nuclear Polarization Enhanced MAS NMR for Structural Analysis of HIV-1 Protein Assemblies.
Dynamic Nuclear Polarization Enhanced MAS NMR for Structural Analysis of HIV-1 Protein Assemblies.
Related Articles Dynamic Nuclear Polarization Enhanced MAS NMR for Structural Analysis of HIV-1 Protein Assemblies.
J Phys Chem B. 2015 Dec 28;
Authors: Gupta R, Lu M, Hou G, Caporini MA, Rosay M, Maas WE, Struppe JO, Suiter CL, Ahn J, Byeon IL, Franks WT, Orwick-Rydmark M, Bertarello A, Oschkinat H, Lesage A, Pintacuda G, Gronenborn AM, Polenova TE
Abstract
Mature infectious HIV-1 virions contain conical capsids comprised of CA...
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12-29-2015 08:05 PM
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.
Structural Analysis of Proteins from Bacterial Secretion Systems and Their Assemblies by NMR Spectroscopy
Linear Mode
