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Molecularand Silica-Supported Molybdenum Alkyne MetathesisCatalysts: Influence of Electronics and Dynamics on Activity Revealedby Kinetics, Solid-State NMR, and Chemical Shift Analysis
Nov 29, 2017 - 9:22 AM - by nmrlearner
nmrlearner's Avatar Molecularand Silica-Supported Molybdenum Alkyne MetathesisCatalysts: Influence of Electronics and Dynamics on Activity Revealedby Kinetics, Solid-State NMR, and Chemical Shift Analysis

Deven P. Estes, Christopher P. Gordon, Alexey Fedorov, Wei-Chih Liao, Henrike Ehrhorn, Celine Bittner, Manuel Luca Zier, Dirk Bockfeld, Ka Wing Chan, Odile Eisenstein, Christophe Raynaud, Matthias Tamm and Christophe Cope?ret



Journal of the American Chemical Society
DOI: 10.1021/jacs.7b09934




Source: Journal of the American Chemical Society
0 Replies | 18 Views
Correctionto “Structure of Colloidal QuantumDots from Dynamic Nuclear Polarization Surface Enhanced NMR Spectroscopy”
Nov 29, 2017 - 9:22 AM - by nmrlearner
nmrlearner's Avatar Correctionto “Structure of Colloidal QuantumDots from Dynamic Nuclear Polarization Surface Enhanced NMR Spectroscopy”

Laura Piveteau, Ta-Chung Ong, Aaron J. Rossini, Lyndon Emsley, Christophe Cope?ret and Maksym V. Kovalenko

Journal of the American Chemical Society
DOI: 10.1021/jacs.7b11716




Source: Journal of the American Chemical Society
0 Replies | 13 Views
Manufacturing Bits: Nov. 28 - SemiEngineering
Nov 28, 2017 - 4:45 PM - by nmrlearner
nmrlearner's Avatar
SemiEngineering


Manufacturing Bits: Nov. 28
SemiEngineering
â??Often times these cannot be crystallized for X-ray crystallography (XRD) or are too large and complex for nuclear magnetic resonance (NMR) spectroscopy. These include many biologically important proteins, especially those with variable or flexible ...



Manufacturing Bits: Nov. 28 - SemiEngineering
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0 Replies | 24 Views
[NMR paper] NMR Spectroscopy Approach to Study the Structure, Orientation, and Mechanism of the Multidrug Exporter EmrE.
Nov 28, 2017 - 4:45 PM - by nmrlearner
nmrlearner's Avatar NMR Spectroscopy Approach to Study the Structure, Orientation, and Mechanism of the Multidrug Exporter EmrE.

NMR Spectroscopy Approach to Study the Structure, Orientation, and Mechanism of the Multidrug Exporter EmrE.

Methods Mol Biol. 2018;1700:83-96

Authors: Leninger M, Traaseth NJ

Abstract
Multidrug exporters are a class of membrane proteins that remove antibiotics from the cytoplasm of bacteria and in the process confer multidrug resistance to the organism. This chapter outlines the sample preparation and optimization of oriented solid-state NMR experiments applied to the study of structure and dynamics for the model transporter EmrE from the small multidrug resistance (SMR) family.


PMID: 29177827 [PubMed - in process]



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0 Replies | 16 Views
[NMR paper] 1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins.
Nov 28, 2017 - 4:45 PM - by nmrlearner
nmrlearner's Avatar 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. Although 13C-detected ssNMR experiments continue to play a major role, recent technological developments have made it possible to carry out 1H-detected experiments, boosting both sensitivity and resolution. Here, we describe a new set of 1H-detected hybrid pulse sequences that combine through-bond and through-space correlation elements into single experiments, enabling the simultaneous detection of rigid and dynamic domains of membrane proteins. As proof-of-principle, we applied these new pulse sequences to the membrane protein phospholamban (PLN) reconstituted in lipid bilayers under moderate MAS conditions. The cross-polarization (CP) based elements enabled the detection of the relatively immobile residues of PLN in the transmembrane domain using through-space correlations; whereas the most dynamic region, which is in equilibrium between folded and unfolded states, was mapped by through-bond INEPT-based elements. These new 1H-detected experiments will enable one to detect not only the most populated (ground) states of biomacromolecules, but also sparsely populated high-energy (excited) states for a complete... [Read More]
0 Replies | 18 Views
Improved strategies for DNP-enhanced 2D 1H-X heteronuclear correlation spectroscopy of surfaces #DNPNMR
Nov 28, 2017 - 3:58 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

Improved strategies for DNP-enhanced 2D 1H-X heteronuclear correlation spectroscopy of surfaces #DNPNMR

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Kobayashi, T., et al., Improved strategies for DNP-enhanced 2D 1H-X heteronuclear correlation spectroscopy of surfaces. Solid State Nucl Magn Reson, 2017. 87(Supplement C): p. 38-44.


https://www.ncbi.nlm.nih.gov/pubmed/28834782


We demonstrate that dynamic nuclear polarization (DNP)-enhanced 1H-X heteronuclear correlation (HETCOR) measurements of hydrogen-rich surface species are better accomplished by using proton-free solvents. This approach notably prevents HETCOR spectra from being obfuscated by the solvent-derived signals otherwise present in DNP measurements. Additionally, in the hydrogen-rich materials studied here, which included functionalized mesoporous silica nanoparticles and metal organic frameworks, the use of proton-free solvents afforded higher sensitivity gains than the commonly used solvents containing protons. We also explored the possibility of using a solvent-free sample formulation and the feasibility of indirect detection in DNP-enhanced HETCOR experiments.
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[NMR] Postdoc in Fast MAS Methods, ETH Zurich
Nov 28, 2017 - 3:58 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[NMR] Postdoc in Fast MAS Methods, ETH Zurich

Postdoctoral Position in NMR Methods developement in the solid-state NMR group of Prof. Beat Meier at ETH Zürich


Our research is centred around solid-state NMR structure determination of biomolecules (fibrils, membrane proteins, protein-DNA complexes). Increasing the presently accessible MAS frequencies (150 kHz) to 200-250 kHz will improve dramatically the spectral quality and will, when successful, lead to a greatly improved resolution in the solid-state NMR spectra of large biological systems, e.g. amyloid fibrils, membrane proteins, virus capsids and proteins assemblies. However, new pulse sequencies will be needed for faster MAS.
The project will focus on the development of novel pulse sequences for assignment and structure determination under fast MAS NMR spectroscopy. The theoretical and numerical spin-dynamics simulation work will be closely linked to experimental verification on model proteins. The experimental work can be started with the equipment presently available in the lab at 110-150 kHz MAS. Spectrometers at 500, 600, 850 (2x) and, in the future 1100 MHz are available. See also http://nmr.ethz.ch


Prerequisites: Ph.D. in Chemistry, Physics, Biology, Interdisciplinary Sciences, or related area, experience in solid-state NMR and NMR methodological development. Motivation to work in a multidisciplinary team.


Applications with motivation letter, CV, publication list, and contact information for 2 references should be sent... [Read More]
0 Replies | 21 Views
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