How proteins switch between various ligand-free and ligand-bound structures has been a key biophysical question ever since the postulation of the Monod-Wyman-Changeux and Koshland-Nemethy-Filmer models over six decades ago. The ability of NMR spectroscopy to provide structural and kinetic information on biomolecular conformational exchange places it in a unique position as an analytical tool to interrogate the mechanisms of biological processes such as protein folding and biomolecular complex...
[NMR paper] Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
Related Articles Elucidating 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...
Study finding could shed light on molecular mechanisms underlying Huntington's disease - News-Medical.net
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Study finding could shed light on molecular mechanisms underlying Huntington's disease
News-Medical.net
... the process," he said. "Using advanced nuclear magnetic resonance spectroscopy, we were able to provide an unprecedented view of the internal structure of the protein clumps that form in the disease, which we hope will one day lead to new therapies ...
Researchers Describe Brain Plaques Involved In...
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Conformational Switching and Nanoscale Assembly ofHuman Prion Protein into Polymorphic Amyloids via Structurally LabileOligomers
Conformational Switching and Nanoscale Assembly ofHuman Prion Protein into Polymorphic Amyloids via Structurally LabileOligomers
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01110/20151217/images/medium/bi-2015-01110g_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01110
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/V02jj6wRm7s
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12-18-2015 07:25 AM
[NMR paper] The Structural Basis of the Green-Blue Color Switching in Proteorhodopsin determined by NMR Spectroscopy.
The Structural Basis of the Green-Blue Color Switching in Proteorhodopsin determined by NMR Spectroscopy.
The Structural Basis of the Green-Blue Color Switching in Proteorhodopsin determined by NMR Spectroscopy.
J Am Chem Soc. 2014 Nov 21;
Authors: Mao J, Do NN, Scholz F, Reggie L, Mehler M, Lakatos A, Ong YS, Ullrich SJ, Brown LJ, Brown RC, Becker-Baldus J, Wachtveitl J, Glaubitz C
Abstract
Proteorhodopsins (PRs) found in marine microbes are the most abundant retinal-based photoreceptors on this planet. PR variants show a high...
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11-23-2014 03:47 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 the mechanisms underlying protein conformational switching using NMR spectroscopy
Linear Mode
