Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org
Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org
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Nanodiscs catch misfolding proteins red-handed - Phys.org
Phys.Org
When proteins misfold, accumulate and clump around insulin-producing cells in the pancreas, they kill cells. Now, researchers, including University of Michigan biophysicists, have obtained a structural snapshot of these proteins ...
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12-06-2017 11:04 PM
[NMR paper] 1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins.
1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins.
1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins.
J Magn Reson. 2017 Dec;285:101-107
Authors: Gopinath T, Nelson SED, Veglia G
Abstract
Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is emerging as a unique method for the atomic resolution structure determination of native membrane proteins in lipid bilayers....
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11-28-2017 04:45 PM
[NMR paper] 1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins
1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins
Publication date: December 2017
Source:Journal of Magnetic Resonance, Volume 285</br>
Author(s): T. Gopinath, Sarah E.D. Nelson, Gianluigi Veglia</br>
Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is emerging as a unique method for the atomic resolution structure determination of native membrane proteins in lipid bilayers. Although 13C-detected ssNMR experiments continue to play a major role, recent technological...
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11-24-2017 05:56 PM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
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Phys.Org
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Light microscopy provides a deep look into protein structure - Phys.org
Phys.Org
Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ...
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01-25-2017 11:13 PM
[NMR paper] Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis.
Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis.
Related Articles Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis.
J Biomol NMR. 2016 Jan 6;
Authors: Yang Y, Huang F, Huber T, Su XC
Abstract
Design of a paramagnetic metal binding motif in a protein is a valuable way for understanding the function, dynamics and interactions of a protein by paramagnetic...
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01-07-2016 11:10 PM
Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis
Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis
Abstract
Design of a paramagnetic metal binding motif in a protein is a valuable way for understanding the function, dynamics and interactions of a protein by paramagnetic NMR spectroscopy. Several strategies have been proposed to site-specifically tag proteins with paramagnetic lanthanide ions. Here we report a simple approach of engineering a transition metal binding motif via site-specific labelling of a...
Joining proteins together with rigid links - Phys.Org
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