New interaction mechanism of proteins discovered | EurekAlert ... - EurekAlert (press release)
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New interaction mechanism of proteins discovered | EurekAlert ...
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UZH researchers have discovered a previously unknown way in which proteins interact with one another and cells organize themselves. This new mechanism involves two fully unstructured proteins forming an ultra-high-affinity complex due to their opposite ...
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New interaction mechanism of proteins discovered | EurekAlert ... - EurekAlert (press release)
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02-22-2018 02:13 AM
Discovery puts the brakes on HIV's ability to infect | EurekAlert ... - EurekAlert (press release)
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Discovery puts the brakes on HIV's ability to infect | EurekAlert ...
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In a study led by the University of Delaware and the University of Pittsburgh School of Medicine, researchers discovered a 'brake' that interferes with HIV's development into an infectious agent. This mechanism prevents the capsid -- the protein shell ...
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Discovery puts the brakes...
nmrlearner
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12-01-2017 08:23 AM
Evolutionary advantage of the common periwinkle | EurekAlert ... - EurekAlert (press release)
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Evolutionary advantage of the common periwinkle | EurekAlert ...
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A special kind of small sulfur-rich proteins, the metallothioneins, have an extraordinarily large capability for binding heavy metals. An international team of ...
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03-24-2017 10:14 PM
Study shows how mutations disrupt ALS-linked protein | EurekAlert ... - EurekAlert (press release)
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Study shows how mutations disrupt ALS-linked protein | EurekAlert ...
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Structural biologists provide a new explanation for how ALS-associated genetic flaws interfere with the proper function and behavior of the protein TDP-43.
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Study shows how mutations disrupt ALS-linked protein | EurekAlert ... - EurekAlert (press release)
nmrlearner
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08-19-2016 04:05 AM
[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 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...