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Resolving Interfacial Protein Dynamics by STReM - Brinkwire (press release)
Feb 18, 2018 - 5:54 AM - by nmrlearner
nmrlearner's Avatar Resolving Interfacial Protein Dynamics by STReM - Brinkwire (press release)



Resolving Interfacial Protein Dynamics by STReM
Brinkwire (press release)
Protein separations are getting increasingly important as the pharmaceutical industry moves away from organic molecules as therapeutics. The industry is moving towards therapeutics that are often proteins or peptides or sometimes they're DNA or RNA ...


Read here
0 Replies | 3 Views
[NMR paper] Solid-state [13C-15N] NMR resonance assignment of hepatitis B virus core protein.
Feb 18, 2018 - 5:54 AM - by nmrlearner
nmrlearner's Avatar Solid-state [13C-15N] NMR resonance assignment of hepatitis B virus core protein.

Related Articles Solid-state [13C-15N] NMR resonance assignment of hepatitis B virus core protein.

Biomol NMR Assign. 2018 Feb 16;:

Authors: Lecoq L, Wang S, Wiegand T, Bressanelli S, Nassal M, Meier BH, Böckmann A

Abstract
Each year, nearly 900,000 deaths are due to serious liver diseases caused by chronic hepatitis B virus infection. The viral particle is composed of an outer envelope and an inner icosahedral nucleocapsid formed by multiple dimers of a ~ 20*kDa self-assembling core protein (Cp). Here we report the solid-state 13C and 15N resonance assignments of the assembly domain, Cp149, of the core protein in its capsid form. A secondary chemical shift analysis of the 140 visible residues suggests an overall alpha-helical three-dimensional fold matching that derived for Cp149 from the X-ray crystallography of the capsid, and from solution-state NMR of the Cp149 dimer. Interestingly, however, at three distinct regions the chemical shifts in solution differ significantly between core proteins in the capsid state versus in the dimer state, strongly suggesting the respective residues to be involved in capsid assembly.


PMID: 29450824 [PubMed - as supplied by publisher]



... [Read More]
0 Replies | 3 Views
[NMR paper] NMR resonance assignments of RNase P protein from Thermotoga maritima.
Feb 18, 2018 - 5:54 AM - by nmrlearner
nmrlearner's Avatar NMR resonance assignments of RNase P protein from Thermotoga maritima.

Related Articles NMR resonance assignments of RNase P protein from Thermotoga maritima.

Biomol NMR Assign. 2018 Feb 15;:

Authors: Zeng D, Brown BP, Voehler MW, Cai S, Reiter NJ

Abstract
Ribonuclase P (RNase P) is an essential metallo-endonuclease that catalyzes 5' precursor-tRNA (ptRNA) processing and exists as an RNA-based enzyme in bacteria, archaea, and eukaryotes. In bacteria, a large catalytic RNA and a small protein component assemble to recognize and accurately cleave ptRNA and tRNA-like molecular scaffolds. Substrate recognition of ptRNA by bacterial RNase P requires RNA-RNA shape complementarity, intermolecular base pairing, and a dynamic protein-ptRNA binding interface. To gain insight into the binding specificity and dynamics of the bacterial protein-ptRNA interface, we report the backbone and side chain 1H, 13C, and 15N resonance assignments of the hyperthermophilic Thermatoga maritima RNase P protein in solution at 318*K. Our data confirm the formation of a stable RNA recognition motif (RRM) with intrinsic heterogeneity at both the N- and C-terminus of the protein, consistent with available structural information. Comprehensive resonance assignments of the bacterial RNase P protein serve as an important first step in understanding how coupled RNA binding and protein-RNA conformational changes give rise to... [Read More]
0 Replies | 3 Views
Pacific Northwest National Laboratory, OHSU Create Joint Research Co-Laboratory to Advance Precision Medicine - Lab Manager Magazine
Feb 16, 2018 - 3:50 PM - by nmrlearner
nmrlearner's Avatar
Lab Manager Magazine


Pacific Northwest National Laboratory, OHSU Create Joint Research Co-Laboratory to Advance Precision Medicine
Lab Manager Magazine
Scientists at PNNL use state-of-the-art nuclear magnetic resonance capabilities to conduct proteomic research such as identifying breast cancer suppressor proteins. The Lab is teaming with OHSU to form the Precision Medicine Innovation Co-Laboratory ...

and more »
... [Read More]
0 Replies | 9 Views
NMR Signal Quenching from Bound Biradical Affinity Reagents in DNP Samples #DNPNMR #NMR
Feb 16, 2018 - 3:50 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

NMR Signal Quenching from Bound Biradical Affinity Reagents in DNP Samples #DNPNMR #NMR

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Rogawski, R., et al., NMR Signal Quenching from Bound Biradical Affinity Reagents in DNP Samples. J Phys Chem B, 2017. 121(48): p. 10770-10781.


https://www.ncbi.nlm.nih.gov/pubmed/29116793


We characterize the effect of specifically bound biradicals on the NMR spectra of dihydrofolate reductase from E. coli. Dynamic nuclear polarization methods enhance the signal-to-noise of solid state NMR experiments by transferring polarization from unpaired electrons of biradicals to nuclei. There has been recent interest in colocalizing the paramagnetic polarizing agents with the analyte of interest through covalent or noncovalent specific interactions. This experimental approach broadens the scope of dynamic nuclear polarization methods by offering the possibility of selective signal enhancements and the potential to work in a broad range of environments. Paramagnetic compounds can have other effects on the NMR spectroscopy of nearby nuclei, including broadening of nuclear resonances due to the proximity of the paramagnetic agent. Understanding the distance dependence of these interactions is important for the success of the technique. Here we explore paramagnetic signal quenching due to a bound biradical, specifically a biradical-derivatized trimethoprim ligand of E. coli dihydrofolate reductase. Biradical-derivatized trimethoprim has nanomolar affinity for its target, and affords strong... [Read More]
0 Replies | 8 Views
[NMR] PhD position at the CNRS/University of Marseille #DNPNMR
Feb 16, 2018 - 3:50 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[NMR] PhD position at the CNRS/University of Marseille #DNPNMR



ERC-funded PhD position is available in Marseille on the structural investigation of functional organic materials by DNP and NMR


Project title: “Structural investigation of polymorphic organic powders at natural isotopic abundance”


A 3-year PhD position is available at the CNRS/University of Aix-Marseille on the development of new experimental and theoretical approaches in dynamic nuclear polarization (DNP) NMR for the structural investigation of functional organic powders at natural isotopic abundance.


Context: Functional organic materials have been successfully used as active components in many applications, going from light emitters to optical devices, flexible photovoltaic devices, printed electronic inks, molecular machines, pigments, pharmaceuticals, etc. Such compounds can be used to produce low-cost, easily manufacturable, and lightweight materials that can replace traditional inorganic functional materials in energy-related applications (e.g. as semiconductors in solar cells or light emitter diodes), bringing significant economic and practical benefits. Moreover, they can be easily chemically modified to respond to specific application requirements (e.g. as active principle ingredients in pharmacy). In view of obtaining new functional materials with tailored properties, the true challenge in this field is the ability to establish a clear two-way relationship between the structure and the properties of the functional material in its end-use solid form. Because, in their end-use form, materials for the mentioned applications generally form particles with nanometer to micrometer-size dimensions, the... [Read More]
0 Replies | 8 Views
Magnetic benchmark: Record-breaking thin film
Feb 15, 2018 - 9:37 AM - by nmrlearner
nmrlearner's Avatar Magnetic benchmark: Record-breaking thin film

US researchers have developed a new magnetic thin film that could finally break through the Slater-Pauling limit on magnetic density in a material. With this decades-old benchmark circumvented new applications and devices might be possible.

Read the rest at Spectroscopynow.com
0 Replies | 11 Views
Photo-induced radical polarization and liquid-state dynamic nuclear polarization using fullerene nitroxide derivatives #DNPNMR
Feb 14, 2018 - 4:47 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

Photo-induced radical polarization and liquid-state dynamic nuclear polarization using fullerene nitroxide derivatives #DNPNMR

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Liu, G., et al., Photo-induced radical polarization and liquid-state dynamic nuclear polarization using fullerene nitroxide derivatives. Phys. Chem. Chem. Phys., 2017. 19(47): p. 31823-31829.


https://www.ncbi.nlm.nih.gov/pubmed/29171613


We report on radical polarization and optically-driven liquid DNP using nitroxide radicals functionalized by photoexcitable fullerene derivatives. Pulse laser excitation of the fullerene moiety leads to transient nitroxide radical polarization that is one order of magnitude larger than that at the Boltzmann equilibrium. The life time of the radical polarization increases with the size of the fullerene derivative and is correlated with the electronic spin-lattice relaxation time T1e. Overhauser NMR signal enhancements of toluene solvent protons were observed under steady-state illumination, which replaced microwave irradiation.
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Go to The DNP-NMR Blog for more info.
0 Replies | 11 Views
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