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Nano 'sushi' catch toxic amyloids in action - Futurity - Futurity: Research News
Dec 06, 2017 - 11:04 PM - by nmrlearner
nmrlearner's Avatar
Futurity: Research News


Nano 'sushi' catch toxic amyloids in action - Futurity
Futurity: Research News
Clumps of misfolded proteins, called plaques or amyloid fibers, are implicated in many diseases: Alzheimer's, Parkinson's, and type 2 diabetes.

and more »

Nano 'sushi' catch toxic amyloids in action - Futurity - Futurity: Research News
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Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org
Dec 06, 2017 - 11:04 PM - by nmrlearner
nmrlearner's Avatar Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org



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 ...

and more »
Read here
0 Replies | 47 Views
[NMR paper] Selenium and Selenocysteine in Protein Chemistry
Dec 06, 2017 - 11:04 PM - by nmrlearner
nmrlearner's Avatar Selenium and Selenocysteine in Protein Chemistry


Selenocysteine, the selenium-containing analogue of cysteine, is the twenty-first proteinogenic amino acid. Since its discovery almost fifty years ago, it has been exploited in unnatural systems even more often than in natural systems. Selenocysteine chemistry has attracted the attention of many chemists in the field of chemical biology owing to its high reactivity and resulting potential for various applications such as chemical modification, chemical protein (semi)synthesis, and protein folding, to name a few. In this Minireview, we will focus on the chemistry of selenium and selenocysteine and their utility in protein chemistry.Se how far we've come: Since its presence in proteins was discovered over 40 years ago, the singular properties of selenocysteine (Sec) have been exploited by protein chemists for a host of different applications. This Minireview summarizes the use of selenium and selenocysteine in various protein chemistry applications, including chemical modifications, protein synthesis, and protein folding.

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0 Replies | 93 Views
A sub-Kelvin cryogen-free EPR system
Dec 06, 2017 - 11:04 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

A sub-Kelvin cryogen-free EPR system

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This article has nothing to do with DNP. However, the article nicely describes an impressive piece of isntrumentation to reach very low temperatures.




Melhuish, S.J., et al., A sub-Kelvin cryogen-free EPR system. J. Magn. Reson., 2017. 282(Supplement C): p. 83-88.


http://www.sciencedirect.com/science...90780717301829


We present an EPR instrument built for operation at Q band below 1K. Our cryogen-free Dewar integrates with a commercial electro-magnet and bridge. A description of the cryogenic and RF systems is given, along with the adaptations to the standard EPR experiment for operation at sub-Kelvin temperatures. As a first experiment, the EPR spectra of powdered Cr12O9(OH)3(O2CCMe3)15 were measured. The sub-Kelvin EPR spectra agree well with predictions, and the performance of the sub-Kelvin system at 5K is compared to that of a commercial spectrometer.
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Go to The DNP-NMR Blog for more info.
0 Replies | 36 Views
Nanodiscs catch misfolding proteins - Xinhua
Dec 06, 2017 - 8:02 AM - by nmrlearner
nmrlearner's Avatar Nanodiscs catch misfolding proteins - Xinhua



Nanodiscs catch misfolding proteins
Xinhua
"We're able to stop the aggregation of the protein in this restricted membrane environment so we can monitor what it looks like before it becomes a mass of fibers," said lead researcher Ayyalusamy Ramamoorthy, UM professor of biophysics and chemistry ...


Read here
0 Replies | 31 Views
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR [Biophysics and Computational Biology]
Dec 06, 2017 - 8:02 AM - by nmrlearner
nmrlearner's Avatar Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR [Biophysics and Computational Biology]

Matthew R. Elkins, Jonathan K. Williams, Martin D. Gelenter, Peng Dai, Byungsu Kwon, Ivan V. Sergeyev, Bradley L. Pentelute, Mei Hong...
Date: 2017-12-05

The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol with M2, as with most eukaryotic membrane proteins, has long been elusive. We have now determined the cholesterol-binding site of... Read More


PNAS:
Number: 49
Volume: 114
0 Replies | 47 Views
[NMR paper] A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation
Dec 06, 2017 - 8:02 AM - by nmrlearner
nmrlearner's Avatar A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation


Metalloproteins utilize O2 as an oxidant, and they often achieve a 4-electron reduction without H2O2 or oxygen radical release. Several proteins have been designed to catalyze one or two-electron oxidative chemistry, but the de novo design of a protein that catalyzes the net 4-electron reduction of O2 has not been reported yet. We report the construction of a diiron-binding four-helix bundle, made up of two different covalently linked ?2 monomers, through click chemistry. Surprisingly, the prototype protein, DF-C1, showed a large divergence in its reactivity from earlier DFs (DF: due ferri, two iron). DFs release the quinone imine and free H2O2 in the oxidation of 4-aminophenol in the presence of O2, whereas FeIII-DF-C1 sequesters the quinone imine into the active site, and catalyzes inside the scaffold an oxidative coupling between oxidized and reduced 4-aminophenol. The asymmetry of the scaffold allowed a fine-engineering of the substrate binding pocket, that ensures selectivity.Not just a four-helix bundle: The use of a diiron-binding four-helix bundle scaffold with an asymmetric active site leads to an enhancement in the selectivity of the iron-catalyzed oxidative coupling of phenols. The stabilization of the oxidized intermediate in the binding pocket enables the net four-electron O2 reduction, without release of any detectable H2O2.

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0 Replies | 51 Views
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