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] Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.
Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.
Related Articles Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.
Angew Chem Int Ed Engl. 2016 May 9;
Authors: Lopez J, Schneider R, Cantrelle FX, Huvent I, Lippens G
Abstract
Under physiological conditions, studies of intrinsically disordered proteins (IDPs) by conventional NMR methods based...
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05-10-2016 04:13 PM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 06:00 AM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 05:59 AM
[NMR paper] Photo-CIDNP NMR methods for studying protein folding.
Photo-CIDNP NMR methods for studying protein folding.
Related Articles Photo-CIDNP NMR methods for studying protein folding.
Methods. 2004 Sep;34(1):75-87
Authors: Mok KH, Hore PJ
Chemically induced dynamic nuclear polarization (CIDNP) is a nuclear magnetic resonance phenomenon that can be used to probe the solvent-accessibility of tryptophan, tyrosine, and histidine residues in proteins by means of laser-induced photochemical reactions, resulting in significant enhancement of NMR signals. CIDNP offers good sensitivity as a surface probe of...
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11-24-2010 10:01 PM
[NMR paper] Studying excited states of proteins by NMR spectroscopy.
Studying excited states of proteins by NMR spectroscopy.
Related Articles Studying excited states of proteins by NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):932-5
Authors: Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE
Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly....
Old methods prove true for studying proteins - Phys.org
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