[NMR paper] A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation.
A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation.
A Functional NMR for Membrane Proteins: Dynamics, Ligand Binding, and Allosteric Modulation.
Protein Sci. 2016 Mar 1;
Authors: Oxenoid K, Chou JJ
Abstract
By nature of conducting ions, transporting substrates and transducing signals, membrane channels, transporters and receptors are expected to exhibit intrinsic conformational dynamics. It is therefore of great interest and importance to understand the various properties of...
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03-02-2016 07:20 PM
[NMR paper] Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
J Biomol NMR. 2016 Feb 2;
Authors: Tang W, Bhatt A, Smith AN, Crowley PJ, Brady LJ, Long JR
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium...
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02-04-2016 11:46 AM
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure comprised of intact P1 covalently attached to the...
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02-02-2016 08:58 PM
[NMR paper] Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
Adv Exp Med Biol. 2015;842:217-30
Authors: Zhang Y, Yamaguchi T, Satoh T, Yagi-Utsumi M, Kamiya Y,...
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05-02-2015 09:41 PM
[NMR paper] Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation.
Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation.
Related Articles Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation.
Biophys J. 2015 Apr 21;108(8):1987-1996
Authors: Weber DK, Yao S, Rojko N, Anderluh G, Lybrand TP, Downton MT, Wagner J, Separovic F
Abstract
Equinatoxin II (EqtII) is a soluble, 20*kDa pore-forming protein toxin isolated from the sea anemone Actinia equina. Although pore formation has long been known to occur...
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Aug;1808(8):2019-30
Authors: Romo TD, Bradney LA, Greathouse DV, Grossfield A
Abstract
One approach to the growing health problem of antibiotic resistant bacteria is the development of antimicrobial peptides (AMPs) as alternative treatments. The...
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08-19-2011 02:56 PM
[NMR paper] Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimension
Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin.
Related Articles Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin.
Biochim Biophys Acta. 2003 Oct 13;1616(2):127-36
Authors: Saitô H, Yamamoto K, Tuzi S, Yamaguchi S
We have recorded...
Specific Lipid Binding of Membrane Proteins in DetergentMicelles Characterized by NMR and Molecular Dynamics
Linear Mode
