Bacterial Filamentous Appendages Investigated by Solid-State NMR Spectroscopy.
Methods Mol Biol. 2017;1615:415-448
Authors: Habenstein B, Loquet A
Abstract
The assembly of filamentous appendages at the surface of bacteria is essential in many infection mechanisms. The extent of mechanical, dynamical, and functional properties of such appendages is very diverse, ranging from a structural scaffold of the pathogen-host cell interaction to cell motility, surface adhesion, or the export of virulence effectors. In particular, the architectures of several bacterial secretion systems have revealed the presence of filamentous architectures, known as pili, fimbriae, andneedles. At the macroscopic level, filamentous bacterial appendages appear as thin extracellular filaments of several nanometers in diameter and up to several microns in length. The structural characterization of these appendages at atomic-scale resolution represents an extremely challenging task because of their inherent noncrystallinity and very poor solubility. Here, we describe protocols based on recent advances in solid-state NMR spectroscopy to investigate the secondary structure, subunit-subunit protein interactions, symmetry parameters, and atomic architecture of bacterial filaments.
[NMR paper] Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
Related Articles Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
J Mol Biol. 2017 May 20;:
Authors: Mandala VS, Liao SY, Kwon B, Hong M
Abstract
The influenza M2 protein forms an acid-activated proton channel that is essential for virus replication. The transmembrane H37 selects for protons under low external pH (pHout) while W41...
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[NMR paper] Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
Biochim Biophys Acta. 2016 Sep 11;
Authors: Chegeni FA, Perin G, Gupta KB, Simionato D, Morosinotto T, Pandit A
Abstract
Photosynthetic thylakoid membranes contain the protein...
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09-22-2016 06:31 AM
[NMR paper] Cellulose Structural Polymorphism in Plant Primary Cell Walls Investigated by High-Field 2D Solid-State NMR Spectroscopy and Density Functional Theory Calculations.
Cellulose Structural Polymorphism in Plant Primary Cell Walls Investigated by High-Field 2D Solid-State NMR Spectroscopy and Density Functional Theory Calculations.
Cellulose Structural Polymorphism in Plant Primary Cell Walls Investigated by High-Field 2D Solid-State NMR Spectroscopy and Density Functional Theory Calculations.
Biomacromolecules. 2016 May 18;
Authors: Wang T, Yang H, Kubicki JD, Hong M
Abstract
The native cellulose of bacterial, algal, and animal origins has been well studied structurally using X-ray and neutron...
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05-19-2016 10:13 AM
[NMR paper] The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.
J Biomol NMR. 2015 Jan 6;
Authors: Thomas L, Kahr J, Schmidt P, Krug U, Scheidt HA, Huster D
Abstract
In contrast to the static snapshots provided by protein crystallography, G protein-coupled receptors constitute a group of proteins with highly dynamic...
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The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy
Abstract
In contrast to the static snapshots provided by protein crystallography, G protein-coupled receptors constitute a group of proteins with highly dynamic properties, which are required in the receptorsâ?? function as signaling molecule. Here, the human neuropeptide Y2 receptor was reconstituted into a model membrane composed of monounsaturated phospholipids and solid-state NMR was used to characterize...
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01-05-2015 04:06 PM
[NMR paper] Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.
Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.
PLoS One. 2012;7(10):e47745
Authors: Bertelsen K,...
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04-02-2013 07:23 PM
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
J Phys Chem B. 2011 Aug 1;
Authors: Su Y, Hong M
A challenge in the application of solid-state NMR spectroscopy to membrane proteins and peptides is the relatively broad linewidths compared to solution NMR spectra. To understand the linewidth contributions to membrane protein spectra, we have measured the inhomogeneous and homogeneous...
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08-03-2011 12:00 PM
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Eur Biophys J. 2011 Mar;40(3):221-34
Authors: Straus SK, Scott WR, Schwieters CD, Marvin DA
Filamentous bacteriophages (filamentous bacterial viruses or Inovirus) are simple and well-characterised macromolecular assemblies that are widely used in molecular biology and biophysics, both as paradigms for studying basic biological questions and as...
Bacterial Filamentous Appendages Investigated by Solid-State NMR Spectroscopy.
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