Related ArticlesElucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
Curr Opin Struct Biol. 2019 Mar 20;57:103-109
Authors: Elkins MR, Hong M
Abstract
Magic-angle-spinning (MAS) solid-state NMR spectroscopy is a versatile technique to elucidate functionally important protein-ligand interactions in lipid membranes. Here, we review recent solid-state NMR studies of membrane protein interactions with cholesterol, lipids, transported substrates, and peptide ligands. These studies are conducted in synthetic or native lipid bilayers to provide an accurate environment for ligand binding. The solid-state NMR approaches include multinuclear detection to gain comprehensive structural information, distance measurements to locate ligand-binding sites, and dynamic nuclear polarization and 1H detection to enhance spectral sensitivity. These studies provide novel insights into the mechanisms of virus budding, virus entry into cells, transmembrane signaling, substrate transport, antibacterial action, and many other biological processes.
PMID: 30903830 [PubMed - as supplied by publisher]
[NMR paper] Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.
Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.
Methods Mol Biol. 2018;1688:37-53
Authors: Gopinath T, Veglia G
Abstract
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11-21-2017 10:10 PM
The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218â??289): a solid-state NMR study
The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218â??289): a solid-state NMR study
Abstract
We have previously shown that Congo red (CR) binds site specifically to amyloid fibrils formed by HET-s(218â??289) with the long axis of the CR molecule almost parallel to the fibril axis. HADDOCK docking studies indicated that CR adopts a roughly planar conformation with the torsion angle Ï? characterizing the relative orientation of the two phenyl rings being a few degrees. In this study, we experimentally determine the torsion angle...
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11-01-2017 07:49 PM
[NMR paper] Solid-state NMR structures of integral membrane proteins.
Solid-state NMR structures of integral membrane proteins.
Related Articles Solid-state NMR structures of integral membrane proteins.
Mol Membr Biol. 2016 Feb 8;:1-23
Authors: Patching SG
Abstract
Solid-state NMR is unique for its ability to obtain three-dimensional structures and to measure atomic-resolution structural and dynamic information for membrane proteins in native lipid bilayers. An increasing number and complexity of integral membrane protein structures have been determined by solid-state NMR using two main methods....
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02-10-2016 09:28 PM
[NMR paper] Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Sci Rep. 2013 Aug 29;3:2538
Authors: Yamamoto K, Dürr UH, Xu J, Im SC, Waskell L, Ramamoorthy A
Abstract
Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as...
Solid-state magic-angle spinning NMR of membrane proteins and proteinligand interactions
Solid-state magic-angle spinning NMR of membrane proteins and proteinligand interactions
April 2012
Publication year: 2012
Source:European Journal of Cell Biology, Volume 91, Issue 4</br>
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Structural biology is developing into a universal tool for visualizing biological processes in space and time at atomic resolution. The field has been built by established methodology like X-ray crystallography, electron microscopy and solution NMR and is now incorporating new techniques, such as small-angle X-ray scattering, electron tomography, magic-angle-spinning solid-state...
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02-03-2013 10:13 AM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Abstract We developed a new method to elucidate the binding kinetics kon and koff, and the dissociation constant KD (=koff/kon), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular weight in a complex with a large target protein. In our method, kon and koff rates are calculated from the analysis of longitudinal relaxation rates of free resonances measured for multiple samples containing different...
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06-06-2011 12:53 AM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
J Biomol NMR. 2011 May 28;
Authors: Sugase K
We developed a new method to elucidate the binding kinetics k(on) and k(off), and the dissociation constant K(D) (=k(off)/k(on)), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular...
Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
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