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New interaction mechanism of proteins discovered | EurekAlert ... - EurekAlert (press release)
Feb 22, 2018 - 2:13 AM - by nmrlearner
nmrlearner's Avatar

New interaction mechanism of proteins discovered | EurekAlert ...
EurekAlert (press release)
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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A quasi-optical and corrugated waveguide microwave transmission system for simultaneous dynamic nuclear polarization NMR on two separate 14.1 T spectrometers #DNPNMR
Feb 22, 2018 - 2:13 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

A quasi-optical and corrugated waveguide microwave transmission system for simultaneous dynamic nuclear polarization NMR on two separate 14.1 T spectrometers #DNPNMR

Gyrotrons typically generate much more microwave power than needed in a DNP-NMR experiment. This article describes a very nice way how to share the microwave power generated by a single gyrotron between two NMR experiments.




Dubroca, T., et al., A quasi-optical and corrugated waveguide microwave transmission system for simultaneous dynamic nuclear polarization NMR on two separate 14.1 T spectrometers. J. Magn. Reson., 2018.


https://www.sciencedirect.com/scienc...90780718300387


Nuclear magnetic resonance (NMR) is an intrinsically insensitive technique, with Boltzmann distributions of nuclear spin states on the order of parts per million in conventional magnetic fields. To overcome this limitation, dynamic nuclear polarization (DNP) can be used to gain up to three orders of magnitude in signal enhancement, which can decrease experimental time by up to six orders of magnitude. In DNP experiments, nuclear spin polarization is enhanced by transferring the relatively larger electron polarization to NMR active nuclei via microwave irradiation. Here, we describe the design and performance of a quasi-optical system enabling the use of a single 395 GHz gyrotron microwave source to simultaneously perform DNP experiments on two different 14.1 T (1H 600 MHz) NMR spectrometers:... [Read More]
0 Replies | 2 Views
[NMR paper] NMR analysis of substrate binding to a two-domain chitinase: Comparison between soluble and insoluble chitins.
Feb 21, 2018 - 1:16 PM - by nmrlearner
nmrlearner's Avatar NMR analysis of substrate binding to a two-domain chitinase: Comparison between soluble and insoluble chitins.

Related Articles NMR analysis of substrate binding to a two-domain chitinase: Comparison between soluble and insoluble chitins.

Carbohydr Res. 2018 Feb 08;458-459:52-59

Authors: Takashima T, Ohnuma T, Fukamizo T

Abstract
CJP-4 is a two-domain chitinase from Japanese cedar (Cryptomeria japonica) pollen, consisting of an N-terminal CBM18 domain and a GH19 catalytic domain. The substrate binding to an inactive mutant protein of full-length CJP-4, in which the catalytic acid Glu108 was mutated to glutamine, CJP-4(E108Q), was analyzed by NMR spectroscopy. Based on the chemical shift perturbations of 1H-15N HSQC signals of Gly26 (CBM18 domain) and Trp185 (GH19 domain), the association constants for individual domains of CJP-4(E108Q) toward soluble chitin hexamer (GlcNAc)6 were determined to be 2300 and 3500 M-1, respectively. Isothermal titration calorimetry provided a similar association constant for (GlcNAc)6 (1980 M-1) with the one-site binding model. One (GlcNAc)6 molecule appeared to bind to a single binding site of CJP-4(E108Q), spanning from CBM18 to GH19 domains. When chitin nanofibers, insoluble chitinase substrate, were added to the CJP-4(E108Q) solution, strong line-broadening was observed for the majority of the backbone resonances in CBM18 domain but not in GH19 domain, indicating a binding preference of CBM18 domain to the insoluble chitin. We here... [Read More]
0 Replies | 8 Views
[NMR paper] NMR metabolomics highlights sphingosine kinase-1 as a new molecular switch in the orchestration of aberrant metabolic phenotype in cancer cells.
Feb 21, 2018 - 1:16 PM - by nmrlearner
nmrlearner's Avatar NMR metabolomics highlights sphingosine kinase-1 as a new molecular switch in the orchestration of aberrant metabolic phenotype in cancer cells.

Related Articles NMR metabolomics highlights sphingosine kinase-1 as a new molecular switch in the orchestration of aberrant metabolic phenotype in cancer cells.

Mol Oncol. 2017 May;11(5):517-533

Authors: Bernacchioni C, Ghini V, Cencetti F, Japtok L, Donati C, Bruni P, Turano P

Abstract
Strong experimental evidence in animal and cellular models supports a pivotal role of sphingosine kinase-1 (SK1) in oncogenesis. In many human cancers, SK1 levels are upregulated and these increases are linked to poor prognosis in patients. Here, by employing untargeted NMR-based metabolomic profiling combined with functional validations, we report the crucial role of SK1 in the metabolic shift known as the Warburg... [Read More]
0 Replies | 7 Views
[NMR paper] Substrate binding drives active site closing of human blood group B galactosyltransferase as revealed by hot-spot labeling and NMR experiments.
Feb 21, 2018 - 12:45 AM - by nmrlearner
nmrlearner's Avatar Substrate binding drives active site closing of human blood group B galactosyltransferase as revealed by hot-spot labeling and NMR experiments.

Related Articles Substrate binding drives active site closing of human blood group B galactosyltransferase as revealed by hot-spot labeling and NMR experiments.

Chembiochem. 2018 Feb 19;:

Authors: Peters T, Weissbach S, Flügge F


Abstract
Crystallography has shown that human blood group A (GTA) and B (GTB) glycosyltransferases undergo transitions between "open", "semi-closed", and "closed" conformations upon substrate binding. However, the time scales of corresponding conformational reorientations are unknown. Crystal structures show that Trp and Met residues are located at "conformational hot spots" of the enzymes. Therefore, we have utilized 15N-side chain labeling of Trp residues, and 13C-methyl labeling of Met residues to study substrate induced conformational transitions of GTB. Chemical shift perturbations (CSPs) of Met and Trp residues in direct contact with substrate ligands reflect binding kinetics, whereas CSPs of Met and Trp residues at remote sites reflect conformational changes of the enzyme upon substrate binding. Acceptor binding is fast on the chemical shift time scale with rather small CSPs in the range of less than ca. 20 Hz. Donor binding matches the intermediate exchange regime yielding an estimate for exchange rate... [Read More]
0 Replies | 8 Views
[NMR paper] HTS by NMR for the Identification of Potent and Selective Inhibitors of Metalloenzymes.
Feb 21, 2018 - 12:45 AM - by nmrlearner
nmrlearner's Avatar HTS by NMR for the Identification of Potent and Selective Inhibitors of Metalloenzymes.

Related Articles HTS by NMR for the Identification of Potent and Selective Inhibitors of Metalloenzymes.

ACS Med Chem Lett. 2018 Feb 08;9(2):137-142

Authors: Baggio C, Cerofolini L, Fragai M, Luchinat C, Pellecchia M

Abstract
We have recently proposed a novel drug discovery approach based on biophysical screening of focused positional scanning libraries in which each element of the library contained a common binding moiety for the given target or class of targets. In this Letter, we report on the implementation of this approach to target metal containing proteins. In our implementation, we first derived a focused positional scanning combinatorial library of peptide mimetics (of approximately 100,000 compounds) in which each element of the library contained the metal-chelating moiety hydroxamic acid at the C-terminal. Screening of this library by nuclear magnetic resonance spectroscopy in solution allowed the identification of a novel and selective compound series targeting MMP-12. The data supported that our general approach, perhaps applied using other metal chelating agents or other initial binding fragments, may result very effective in deriving novel and selective agents against metalloenzyme.


PMID: 29456802 [PubMed]



... [Read More]
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[nmr] ampere nmr school 2018
Feb 21, 2018 - 12:45 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[NMR] AMPERE NMR SCHOOL 2018

Dear NMR Community,


On behalf of the Organizing Committee it’s my great pleasure to invite you to attend the next AMPERE NMR School 2018, an annual event organized since earlier 90th in Zakopane under auspices of the Groupment AMPERE, will be organized from June 10 th to 16 th 2018 in Zakopane, Poland ( www. zakopane .pl).


The traditional topics given in the School:
· solid state and soft matter NMR
· NMR diffusometry and relaxometry
· application of NMR in biology and medicine
· magnetic resonance imaging and spectroscopy
· NMR and quantum information
· theoretical and experimental aspects of dynamic nuclear spin polarization
· NMR methodology and techniques.


The School is addressed to PhD students of various fields of physics, chemistry, biology and medicine and is focused on theoretical and experimental aspects of NMR methods and their applications. The lectures are expected to contain a basic (tutorial) introduction and the research of your interest.


The conference fee (450 Euro) includes full board, accommodation and the conference proceedings. We will be able to provide a financial support for the students you will recommend up to 200 Euro. More detailed information you will find on the conference website.


http://www.staff.amu.edu.pl/~school/fee.html


... [Read More]
0 Replies | 8 Views
[NMR] Open NMR Position at MPI Kohlenforschung in Mülheim an der Ruhr
Feb 21, 2018 - 12:45 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[NMR] Open NMR Position at MPI Kohlenforschung in Mülheim an der Ruhr

A new position in the area NMR applied to catalysis research is now open in Mülheim an der Ruhr, Germany. Please distribute. (Basic German knowledge required ;)


http://www.kofo.mpg.de/de/karriere/s...itarbeiter-in-


---------------------------------------------------
Christophe Farès, Ph.D.
---------------------------------------------------
NMR Department/NMR Abteilung
Max-Planck Insitut für Kohlenforschung/ Max-Planck Insitute for Coal Research
Kaiser-Wilhelm Platz 1
45470 Mülheim an der Ruhr
Tel: +49 208 306 2130
E-mail: fares [a] mpi-muelheim [.] mpg [.] de
---------------------------------------------------


====================================
This is the AMPERE MAGNETIC RESONANCE mailing list:
http://www.drorlist.com/nmrlist.html


NMR web database:
http://www.drorlist.com/nmr.html


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