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1H NMR Spectroscopy of [FeFe] Hydrogenase:Insight into the Electronic Structure of the Active Site
Dec 15, 2017 - 7:54 AM - by nmrlearner
nmrlearner's Avatar 1H NMR Spectroscopy of [FeFe] Hydrogenase:Insight into the Electronic Structure of the Active Site

Sigrun Rumpel, Enrico Ravera, Constanze Sommer, Edward Reijerse, Christophe Fare?s, Claudio Luchinat and Wolfgang Lubitz



Journal of the American Chemical Society
DOI: 10.1021/jacs.7b11196




Source: Journal of the American Chemical Society
0 Replies | 7 Views
Scientists make breakthrough in understanding how Parkinson's ... - iNews
Dec 15, 2017 - 7:54 AM - by nmrlearner
nmrlearner's Avatar
iNews


Scientists make breakthrough in understanding how Parkinson's ...
iNews
Scientists have made a major breakthrough in understanding how Parkinson's disease develops. Researchers have stabilised toxic protein clusters associated.
... [Read More]
0 Replies | 9 Views
Alzheimer's Tau protein forms toxic complexes with cell membranes - EurekAlert (press release)
Dec 15, 2017 - 7:54 AM - by nmrlearner
nmrlearner's Avatar Alzheimer's Tau protein forms toxic complexes with cell membranes - EurekAlert (press release)



Alzheimer's Tau protein forms toxic complexes with cell membranes
EurekAlert (press release)
In collaboration with Professor David Eliezer at Weill Cornell School of Medical Sciences in New York, the researchers used Nuclear Magnetic Resonance (NMR) to gain insight into the structure of Tau in the core of the complexes. This revealed that the ...

and more »
Read here
0 Replies | 9 Views
One flu over: NMR insights
Dec 15, 2017 - 7:54 AM - by nmrlearner
nmrlearner's Avatar One flu over: NMR insights

When you catch influenza, the virus hijacks the inner workings of your cells to make copies of itself. The copies accumulate in viral buds that then break free from the host cell to infect another host. Researchers at Massachusetts Institute of Technology have now used solid-state nuclear magnetic resonance (NMR) spectroscopy to obtain a clear picture of how these buds pinch off from the host cell membrane.

Read the rest at Spectroscopynow.com
0 Replies | 9 Views
[NMR paper] Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain.
Dec 14, 2017 - 12:56 PM - by nmrlearner
nmrlearner's Avatar Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain.

Related Articles Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain.

J Biomol NMR. 2017 Dec 12;:

Authors: Sharaf NG, Brereton AE, Byeon IL, Karplus PA, Gronenborn AM

Abstract
In the original publication of the article, the given name and family name of the author P. Andrew Karplus was published incorrectly. The name should read as "P. Andrew" - Given name and "Karplus" - Family name.


PMID: 29234947 [PubMed - as supplied by publisher]



More...
0 Replies | 9 Views
[NMR paper] An Exhaustive Search Algorithm to Aid NMR-Based Structure Determination of Rotationally Symmetric Transmembrane Oligomers.
Dec 14, 2017 - 12:56 PM - by nmrlearner
nmrlearner's Avatar An Exhaustive Search Algorithm to Aid NMR-Based Structure Determination of Rotationally Symmetric Transmembrane Oligomers.

Related Articles An Exhaustive Search Algorithm to Aid NMR-Based Structure Determination of Rotationally Symmetric Transmembrane Oligomers.

Sci Rep. 2017 Dec 12;7(1):17373

Authors: Yang J, Piai A, Shen HB, Chou JJ

Abstract
Nuclear magnetic resonance (NMR) has been an important source of structural restraints for solving structures of oligomeric transmembrane domains (TMDs) of cell surface receptors and viral membrane proteins. In NMR studies, oligomers are assembled using inter-protomer distance restraints. But, for oligomers that are higher than dimer, these distance restraints all have two-fold directional ambiguity, and resolving such ambiguity often requires time-consuming trial-and-error calculations using restrained molecular dynamics (MD) with simulated annealing (SA). We report an Exhaustive Search algorithm for Symmetric Oligomer (ExSSO), which can perform near-complete search of the symmetric conformational space in a very short time. In this approach, the predetermined protomer model is subject to full angular and spatial search within the symmetry space. This approach, which can be applied to any rotationally symmetric oligomers, was validated using the structures of the Fas death receptor, the HIV-1 gp41 fusion protein, the influenza proton channel, and the MCU pore. The algorithm is able to generate approximate oligomer solutions... [Read More]
0 Replies | 11 Views
[NMR paper] Comparative NMR and NIRS analysis of oxygen-dependent metabolism in exercising finger flexor muscles.
Dec 13, 2017 - 6:15 PM - by nmrlearner
nmrlearner's Avatar Comparative NMR and NIRS analysis of oxygen-dependent metabolism in exercising finger flexor muscles.

Related Articles Comparative NMR and NIRS analysis of oxygen-dependent metabolism in exercising finger flexor muscles.

Am J Physiol Regul Integr Comp Physiol. 2017 Dec 01;313(6):R740-R753

Authors: Bendahan D, Chatel B, Jue T

Abstract
Muscle contraction requires the physiology to adapt rapidly to meet the surge in energy demand. To investigate the shift in metabolic control, especially between oxygen and metabolism, researchers often depend on near-infrared spectroscopy (NIRS) to measure noninvasively the tissue O2 Because NIRS detects the overlapping myoglobin (Mb) and hemoglobin (Hb) signals in muscle, interpreting the data as an index of cellular or vascular O2 requires deconvoluting the relative contribution. Currently, many in the NIRS field ascribe the signal to Hb. In contrast, 1H NMR has only detected the Mb signal in contracting muscle, and comparative NIRS and NMR experiments indicate a predominant Mb contribution. The present study has examined the question of the NIRS signal origin by measuring simultaneously the 1H... [Read More]
0 Replies | 16 Views
Perspectives on paramagnetic NMR from a life sciences infrastructure
Dec 13, 2017 - 6:15 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

Perspectives on paramagnetic NMR from a life sciences infrastructure

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Ravera, E., G. Parigi, and C. Luchinat, Perspectives on paramagnetic NMR from a life sciences infrastructure. J Magn Reson, 2017. 282(Supplement C): p. 154-169.


https://www.ncbi.nlm.nih.gov/pubmed/28844254


The effects arising in NMR spectroscopy because of the presence of unpaired electrons, collectively referred to as "paramagnetic NMR" have attracted increasing attention over the last decades. From the standpoint of the structural and mechanistic biology, paramagnetic NMR provides long range restraints that can be used to assess the accuracy of crystal structures in solution and to improve them by simultaneous refinements through NMR and X-ray data. These restraints also provide information on structure rearrangements and conformational variability in biomolecular systems. Theoretical improvements in quantum chemistry calculations can nowadays allow for accurate calculations of the paramagnetic data from a molecular structural model, thus providing a tool to refine the metal coordination environment by matching the paramagnetic effects observed far away from the metal. Furthermore, the availability of an improved technology (higher fields and faster magic angle spinning) has promoted paramagnetic NMR applications in the fast-growing area of biomolecular solid-state NMR. Major improvements in dynamic nuclear polarization have been recently achieved, especially through the... [Read More]
0 Replies | 13 Views
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