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[ASAP] Nanoscale Phase Segregation in Supramolecular ?-Templating for Hybrid Perovskite Photovoltaics from NMR Crystallography
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar [ASAP] Nanoscale Phase Segregation in Supramolecular ?-Templating for Hybrid Perovskite Photovoltaics from NMR Crystallography

Michael A. Hope?, Toru Nakamura?, Paramvir Ahlawat?, Aditya Mishra?, Manuel Cordova, Farzaneh Jahanbakhshi, Marko Mladenovic?, Rashmi Runjhun, Lena Merten, Alexander Hinderhofer, Brian I. Carlsen, Dominik J. Kubicki, Renana Gershoni-Poranne, Thomas Schneeberger, Loi? C. Carbone, Yuhang Liu, Shaik M. Zakeeruddin, Janusz Lewinski, Anders Hagfeldt, Frank Schreiber, Ursula Rothlisberger, Michael Gra?tzel, Jovana V. Milic?, and Lyndon Emsley



Journal of the American Chemical Society
DOI: 10.1021/jacs.0c11563



Source: Journal of the American Chemical Society
0 Replies | 16 Views
Study reveals evolutionary origins of fold-switching protein - pnas.org
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar Study reveals evolutionary origins of fold-switching protein pnas.org
Study reveals evolutionary origins of fold-switching protein - pnas.org
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0 Replies | 6 Views
[NMR paper] NMR and MD Simulations Reveal the Impact of the V23D Mutation on the Function of Yeast Oligosaccharyltransferase Subunit Ost4.
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar NMR and MD Simulations Reveal the Impact of the V23D Mutation on the Function of Yeast Oligosaccharyltransferase Subunit Ost4.

Related Articles NMR and MD Simulations Reveal the Impact of the V23D Mutation on the Function of Yeast Oligosaccharyltransferase Subunit Ost4.

Glycobiology. 2021 Jan 12;:

Authors: Chaudhary BP, Zoetewey DL, McCullagh MJ, Mohanty S

Abstract
Asparagine-linked glycosylation, also known as N-linked glycosylation, is an essential and highly conserved co- and post-translational protein modification in eukaryotes and some prokaryotes. In the central step of this reaction, a carbohydrate moiety is transferred from a lipid-linked donor to the side-chain of a consensus asparagine in a nascent protein as it is synthesized at the ribosome. Complete loss of oligosaccharyltransferase (OST) function is lethal in eukaryotes. This reaction is carried out by a membrane-associated multi-subunit enzyme, OST, localized in the endoplasmic reticulum (ER). The smallest subunit, Ost4, contains a single membrane-spanning helix that is critical for maintaining stability and activity of OST. Mutation of any residue from Met18 to Ile24 of Ost4 destabilizes the enzyme complex, affecting its activity. Here, we report solution NMR structures and molecular dynamics simulations of Ost4 and Ost4V23D in micelles. Our studies revealed that while the point mutation did not impact the structure of... [Read More]
0 Replies | 10 Views
[NMR paper] Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.

Related Articles Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.

Nat Protoc. 2021 Jan 13;:

Authors: Narasimhan S, Pinto C, Lucini Paioni A, van der Zwan J, Folkers GE, Baldus M

Abstract
For a long time, solid-state nuclear magnetic resonance (ssNMR) has been employed to study complex biomolecular systems at the detailed chemical, structural, or dynamic level. Recent progress in high-resolution and high-sensitivity ssNMR, in combination with innovative sample preparation and labeling schemes, offers novel opportunities to study proteins in their native setting irrespective of the molecular tumbling rate. This protocol describes biochemical preparation schemes to obtain cellular samples of both soluble as well as insoluble or membrane-associated proteins in bacteria. To this end, the protocol is suitable for studying a protein of interest in both whole cells and in cell envelope or isolated membrane preparations. In the first stage of the procedure, an appropriate strain of Escherichia coli (DE3) is transformed with a plasmid of interest harboring the protein of interest under the... [Read More]
0 Replies | 11 Views
[NMR paper] 1H-NMR metabolomics reveals a multitarget action of Crithmum maritimum ethyl acetate extract in inhibiting hepatocellular carcinoma cell growth.
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar 1H-NMR metabolomics reveals a multitarget action of Crithmum maritimum ethyl acetate extract in inhibiting hepatocellular carcinoma cell growth.

Related Articles 1H-NMR metabolomics reveals a multitarget action of Crithmum maritimum ethyl acetate extract in inhibiting hepatocellular carcinoma cell growth.

Sci Rep. 2021 Jan 13;11(1):1259

Authors: Gnocchi D, Del Coco L, Girelli CR, Castellaneta F, Cesari G, Sabbà C, Fanizzi FP, Mazzocca A

Abstract
Hepatocellular carcinoma (HCC) is nowadays the sixth cause of tumour-related deceases worldwide, estimated to become the third in Western countries by 2030. New drugs for HCC treatment still have many adverse effects. Several lines of evidence indicate that plant metabolites offer concrete opportunities for developing new therapeutic strategies for many diseases, including cancer. We previously reported that ethyl acetate extract of a spontaneous edible plant harvested in Apulia, Crithmum maritimum, significantly inhibited cell growth in HCC cells. By 1H-NMR spectroscopy, here we show that Crithmum maritimum ethyl acetate extract counteracts the Warburg effect, by reducing intracellular lactate, inhibits protein anabolism, by decreasing amino acid level, and affects membrane biosynthesis by lowering choline and phosphocholine. Also, we observed an effect on lipid homeostasis, with a reduction in triglycerides, cholesterol, monounsaturated fatty... [Read More]
0 Replies | 10 Views
[NMR paper] NMR-Based Methods for Protein Analysis.
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar NMR-Based Methods for Protein Analysis.

Related Articles NMR-Based Methods for Protein Analysis.

Anal Chem. 2021 Jan 13;:

Authors: Hu Y, Cheng K, He L, Zhang X, Jiang B, Jiang L, Li C, Wang G, Yang Y, Liu M

Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for analyzing protein structure, interaction, and dynamics at atomic resolution and in various sample states including solution state, solid state, and membranous environment. Thanks to rapid NMR methodology development, the past decade has witnessed a growing number of protein NMR studies in complex systems ranging from membrane mimetics to living cells, which pushes the research frontier further toward physiological environments and offers unique insights in elucidating protein functional mechanisms. In particular, in-cell NMR has become a method of choice for bridging the huge gap between structural biology and cell biology. Herein, we review the recent developments and applications of NMR methods for protein analysis in close-to-physiological environments, with special... [Read More]
0 Replies | 7 Views
[NMR paper] Real-Time NMR Spectroscopy for Studying Metabolism.
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar Real-Time NMR Spectroscopy for Studying Metabolism.

Related Articles Real-Time NMR Spectroscopy for Studying Metabolism.

Angew Chem Int Ed Engl. 2020 02 03;59(6):2304-2308

Authors: Alshamleh I, Krause N, Richter C, Kurrle N, Serve H, GĂ¼nther UL, Schwalbe H

Abstract
Current metabolomics approaches utilize cellular metabolite extracts, are destructive, and require high cell numbers. We introduce here an approach that enables the monitoring of cellular metabolism at lower cell numbers by observing the consumption/production of different metabolites over several kinetic data points of up to 48â??hours. Our approach does not influence cellular viability, as we optimized the cellular matrix in... [Read More]
0 Replies | 7 Views
[NMR paper] Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State NMR.
Jan 15, 2021 - 4:25 PM - by nmrlearner
nmrlearner's Avatar Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State NMR.

Related Articles Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State NMR.

ACS Biomater Sci Eng. 2016 May 09;2(5):758-767

Authors: Callone E, Dirè S, Hu X, Motta A

Abstract
This study is devoted to the deep evaluation of processing-induced protein conformation changes by using silk fibroin fibers and their cast films stabilized by different methods as a model. The control of the hierarchical assembling of silk fibroin is the key for finely tuning the biological functions and physical-chemical properties of the final materials for applications in biomedical fields. However, previous methods usually only focused on the change of beta-sheet crystallinity in silk materials, which can not explain a lot of their specific prosperities generated from different processing methods. By using complementary solid-state NMR, together with FTIR and DSC techniques, we for the first time established the correlations between processing conditions and silk fibroin molecular configurations, and experimentally assess the presence and quantify the percentage of the asymmetric 3-fold helical conformation (Silk III) in silk materials, together with their well-known Silk I-like helix/coil dominated and Silk II beta-sheet... [Read More]
0 Replies | 10 Views
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