[NMR paper] Structural Analysis of Proteins from Bacterial Secretion Systems and Their Assemblies by NMR Spectroscopy
Structural Analysis of Proteins from Bacterial Secretion Systems and Their Assemblies by NMR Spectroscopy
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...
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11-06-2023 07:18 PM
[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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07-24-2017 10:10 AM
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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07-04-2017 04:57 AM
[NMR paper] NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
Angew Chem Int Ed Engl. 2016 Nov 16;:
Authors: Stanek J, Andreas LB, Jaudzems K, Cala D, Lalli D, Bertarello A, Schubeis T, Akopjana I, Kotelovica S, Tars K, Pica A, Leone S, Picone D, Xu ZQ, Dixon NE, Martinez D, Berbon M, El Mammeri N, Noubhani...
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11-20-2016 09:20 PM
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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05-25-2016 02:33 PM
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins
Abstract
Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of 1H, 13C, and 15N resonances and structural analysis in fully protonated proteins. We demonstrate that 13C detected 3D experiments are highly efficient and permit assignments of the majority of backbone resonances, as shown in an 89-residue dynein light chain 8, LC8 protein. With these experiments, we...
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11-11-2014 11:57 AM
[NMR paper] Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
Related Articles Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
J Biomol NMR. 2014 Nov 9;
Authors: Guo C, Hou G, Lu X, O'Hare B, Struppe J, Polenova T
Abstract
Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of (1)H, (13)C, and (15)N...
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11-10-2014 10:59 PM
Radio frequency assisted homonuclear recoupling - A Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems
Radio frequency assisted homonuclear recoupling - A Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 18 January 2011</br>
Michal, Leskes , Ümit, Akbey , Hartmut, Oschkinat , Barth-Jan, van Rossum , Shimon, Vega</br>
We present a Floquet theory approach for the analysis of homonuclear recoupling assisted by radio frequency (RF) irradiation of surrounding heteronuclear spins. This description covers a...
Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS ... - ScienceDirect.com
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