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[NMR paper] A Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Co-precipitates using Solid-state NMR Spectroscopy.
Sep 13, 2017 - 8:48 PM - by nmrlearner
nmrlearner's Avatar A Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Co-precipitates using Solid-state NMR Spectroscopy.

Related Articles A Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Co-precipitates using Solid-state NMR Spectroscopy.

Langmuir. 2017 Sep 12;:

Authors: Buckle EL, Roehrich A, Vandermoon B, Drobny GP

Abstract
A biomimetic, peptide-mediated approach to inorganic nanostructure formation is of great interest as an alternative to industrial production methods. To investigate the role of peptide structure on silica (SiO2) and titania (TiO2) morphologies, we use the R5 peptide domain derived from the silaffin protein to produce uniform SiO2 and TiO2 nanostructures from the precursor silicic acid and titanium bis(ammonium lactato)dihydroxide, respectively. The resulting biosilica and biotitania nanostructures are characterized using scanning electron microscopy. To investigate the process of R5-mediated SiO2 and TiO2 formation, we carry out 1D and 2D solid-state NMR (ssNMR) studies on R5 samples with uniformly 13C- and 15N-labeled residues to determine the backbone and side-chain chemical shifts. 13C chemical shift data are in turn used to determine peptide backbone torsion angles and secondary structure for the R5 peptide neat, in silica, and in titania. We are thus able... [Read More]
0 Replies | 20 Views
Gradient reconstitution of membrane proteins for solid-state NMR studies
Sep 13, 2017 - 3:58 AM - by nmrlearner
nmrlearner's Avatar Gradient reconstitution of membrane proteins for solid-state NMR studies

Abstract

We here adapted the GRecon method used in electron microscopy studies for membrane protein reconstitution to the needs of solid-state NMR sample preparation. We followed in detail the reconstitution of the ABC transporter BmrA by dialysis as a reference, and established optimal reconstitution conditions using the combined sucrose/cyclodextrin/lipid gradient characterizing GRecon. We established conditions under which quantitative reconstitution of active protein at low lipid-to-protein ratios can be obtained, and also how to upscale these conditions in order to produce adequate amounts for NMR. NMR spectra recorded on a sample produced by GRecon showed a highly similar fingerprint as those recorded previously on samples reconstituted by dialysis. GRecon sample preparation presents a gain in time of nearly an order of magnitude for reconstitution, and shall represent a valuable alternative in solid-state NMR membrane protein sample preparation.



Source: Journal of Biomolecular NMR
0 Replies | 52 Views
[U. of Ottawa NMR Facility Blog] Optimizing the Signal-to-Noise-Ratio with Spin-Noise Probe Tuning
Sep 13, 2017 - 3:58 AM - by nmrlearner
nmrlearner's Avatar Optimizing the Signal-to-Noise-Ratio with Spin-Noise Probe Tuning

We have all been taught to tune our NMR probes to maximize the pulse power delivered to our sample (or minimize the reflected power back to the amplifier). This prevents damage to the amplifiers and minimizes the duration of 90 pulses at fixed power levels. This is typically done with the spectrometer hardware (eg, "atmm" or "wobb" on a Bruker spectrometer), with a sweep generator and oscilloscope or a dedicated tuning device. Tuning a probe in this way optimizes the transmission of rf to the sample, however, the NMR probe must also detect signals from the sample to be amplified and sent to the receiver. The "receive" function uses a different electronic path compared to the "transmit" function. Since the electronic paths for the "transmit" and "receive" functions are completely different, they are expected to have different tuning characteristics. A probe optimized to transmit rf to the sample is not necessarily optimized to receive the rf NMR... [Read More]
0 Replies | 50 Views
This Is The Closest Look We've Ever Had at The Proteins Linked to Alzheimer's Disease - ScienceAlert
Sep 12, 2017 - 1:45 PM - by nmrlearner
nmrlearner's Avatar This Is The Closest Look We've Ever Had at The Proteins Linked to Alzheimer's Disease - ScienceAlert


ScienceAlert


This Is The Closest Look We've Ever Had at The Proteins Linked to Alzheimer's Disease
ScienceAlert
Extra readings from solid-state nuclear magnetic resonance (NMR) spectroscopy and X-ray diffraction experiments helped to validate the data and the atomic structure, producing a computer rendering that's the most accurate we've ever seen, down to a ...

... [Read More]
0 Replies | 56 Views
[NMR paper] Reversible DNA-protein cross-linking at epigenetic DNA marks
Sep 12, 2017 - 1:45 PM - by nmrlearner
nmrlearner's Avatar Reversible DNA-protein cross-linking at epigenetic DNA marks


5-Formylcytosine (5fC) is an endogenous DNA modification frequently found within regulatory elements of mammalian genes. Although 5fC is an oxidation product of 5-methylcytosine (5mC), the two epigenetic marks show distinct genome-wide distributions and protein affinities, suggesting that they perform different functions in epigenetic signaling. A unique feature of 5fC is the presence of a potentially reactive aldehyde group in its structure. Here, we show that 5fC bases in DNA readily form Schiff base conjugates with Lys side chains of nuclear proteins in vitro and in vivo. These covalent protein-DNA complexes are reversible (t1/2, 1.8 h), suggesting that they contribute to transcriptional regulation and chromatin remodeling. On the other hand, 5fC mediated DNA-protein cross-links, if present at replication forks or actively transcribed regions, may interfere with DNA replication and transcription.

More...
0 Replies | 29 Views
Overhauser-enhanced magnetic resonance elastography
Sep 12, 2017 - 12:56 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

Overhauser-enhanced magnetic resonance elastography

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Salameh, N., et al., Overhauser-enhanced magnetic resonance elastography. NMR in Biomedicine, 2016. 29(5): p. 607-613.


http://dx.doi.org/10.1002/nbm.3499


Magnetic resonance elastography (MRE) is a powerful technique to assess the mechanical properties of living tissue. However, it suffers from reduced sensitivity in regions with short T2 and T2* such as in tissue with high concentrations of paramagnetic iron, or in regions surrounding implanted devices. In this work, we exploit the longer T2* attainable at ultra-low magnetic fields in combination with Overhauser dynamic nuclear polarization (DNP) to enable rapid MRE at 0.0065 T. A 3D balanced steady-state free precession based MRE sequence with undersampling and fractional encoding was implemented on a 0.0065 T MRI scanner. A custom-built RF coil for DNP and a programmable vibration system for elastography were developed. Displacement fields and stiffness maps were reconstructed from data recorded in a polyvinyl alcohol gel phantom loaded with stable nitroxide radicals. A DNP enhancement of 25 was achieved during the MRE sequence, allowing the acquisition of 3D Overhauser-enhanced MRE (OMRE) images with (1.5 2.7 9) mm3 resolution over eight temporal steps and 11 slices in 6 minutes. In conclusion, OMRE at ultra-low magnetic field can be used to detect mechanical waves over short... [Read More]
0 Replies | 28 Views
[NMR] Faculty position at New York University
Sep 12, 2017 - 12:56 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[NMR] Faculty position at New York University

From the Ampere Magnetic Resonance List






Dear Colleagues,

The Department of Chemistry at New York University is soliciting applications for faculty positions in Chemistry. One of the emphasis areas is biophysical chemistry, which may include NMR or EPR. The deadline for the application is Sep 29, 2017. The full search advertisement is copied and pasted below, and can also be found via the link: http://as.nyu.edu/chemistry/recruitment.html


best wishes,
Nate


----

ASSISTANT PROFESSOR

Department of Chemistry
Arts and Science
New York University

The Department of Chemistry at New York University (NYU) invites applications for several tenure-track faculty positions in all areas of Chemistry and Biochemistry, subject to final administrative approval. Successful candidates must have a Ph.D in chemistry or related field and demonstrate the potential to do pioneering research and to teach effectively at the undergraduate and graduate levels. The positions are anticipated to be at the junior level, although exceptional senior level candidates will be considered. The Department of Chemistry is continuing a significant growth plan, including the creation of the Biomedical Chemistry Institute, the Molecular Design Institute, and the addition of numerous senior and junior faculty members. Interested faculty are able to participate in... [Read More]
0 Replies | 43 Views
Protein Structure Determination - News-Medical.net
Sep 11, 2017 - 12:36 PM - by nmrlearner
nmrlearner's Avatar Protein Structure Determination - News-Medical.net



Protein Structure Determination
News-Medical.net
Cryoelectron microscopy is a variant at temperatures at or below that of liquid nitrogen and can visualize protein structures at very high resolution, though is less than that of methods like NMR spectroscopy or crystallography. It works with minute ...


Read here
0 Replies | 48 Views
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