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Discovery Puts the Brakes on HIV's Ability to Infect - Laboratory Equipment
Dec 01, 2017 - 9:24 PM - by nmrlearner
nmrlearner's Avatar
Laboratory Equipment


Discovery Puts the Brakes on HIV's Ability to Infect
Laboratory Equipment
She is an expert in nuclear magnetic resonance (NMR) spectroscopy, which helps scientists identify and pinpoint the location of every atom in a structure and how each atom moves. "Viruses like HIV and their constituent protein and nucleic acid ...

and more »

Discovery Puts the Brakes on HIV's Ability... [Read More]
0 Replies | 18 Views
[NMR paper] High-Confidence Protein-Ligand Complex Modeling by NMR-Guided Docking Enables Early Hit Optimization.
Dec 01, 2017 - 9:24 PM - by nmrlearner
nmrlearner's Avatar High-Confidence Protein-Ligand Complex Modeling by NMR-Guided Docking Enables Early Hit Optimization.

High-Confidence Protein-Ligand Complex Modeling by NMR-Guided Docking Enables Early Hit Optimization.

J Am Chem Soc. 2017 Nov 30;:

Authors: Proudfoot A, Bussiere DE, Lingel A

Abstract
Structure-based drug design is an integral part of modern day drug discovery and requires detailed structural characterization of protein-ligand interactions, which is most commonly performed by X-ray crystallography. However, the success rate of generating these costructures is often variable, in particular when working with dynamic proteins or weakly binding ligands. As a result, structural information is not routinely obtained in these scenarios, and ligand optimization is challenging or not pursued at all, representing a substantial limitation in chemical scaffolds and diversity. To overcome this impediment, we have developed a robust NMR restraint guided docking protocol to generate high-quality models of protein-ligand complexes. By combining the use of highly methyl-labeled protein with experimentally determined intermolecular distances, a comprehensive set of protein-ligand distances is generated which then drives the docking process and enables the determination of the correct ligand conformation in the bound state. For the first time,... [Read More]
0 Replies | 13 Views
Rapid and reliable protein structure determination via chemical shift threading
Dec 01, 2017 - 8:23 AM - by nmrlearner
nmrlearner's Avatar Rapid and reliable protein structure determination via chemical shift threading

Abstract


Protein structure determination using nuclear magnetic resonance (NMR) spectroscopy can be both time-consuming and labor intensive. Here we demonstrate how chemical shift threading can permit rapid, robust, and accurate protein structure determination using only chemical shift data. Threading is a relatively old bioinformatics technique that uses a combination of sequence information and predicted (or experimentally acquired) low-resolution structural data to generate high-resolution 3D protein structures. The key motivations behind using NMR chemical shifts for protein threading lie in the fact that they are easy to measure, they are available prior to 3D structure determination, and they contain vital structural information. The method we have developed uses not only sequence and chemical shift similarity but also chemical shift-derived secondary structure, shift-derived super-secondary structure, and shift-derived accessible surface area to generate a high quality protein structure regardless of the sequence similarity (or lack thereof) to a known structure already in the PDB. The method (called E-Thrifty) was found to be very fast (oftenâ??
0 Replies | 18 Views
High-ConfidenceProtein–Ligand Complex Modelingby NMR-Guided Docking Enables Early Hit Optimization
Dec 01, 2017 - 8:23 AM - by nmrlearner
nmrlearner's Avatar High-ConfidenceProtein–Ligand Complex Modelingby NMR-Guided Docking Enables Early Hit Optimization

Andrew Proudfoot, Dirksen E. Bussiere and Andreas Lingel



Journal of the American Chemical Society
DOI: 10.1021/jacs.7b07171




Source: Journal of the American Chemical Society
0 Replies | 15 Views
17O MAS NMR Correlation Spectroscopy atHigh Magnetic Fields
Dec 01, 2017 - 8:23 AM - by nmrlearner
nmrlearner's Avatar 17O MAS NMR Correlation Spectroscopy atHigh Magnetic Fields

Eric G. Keeler, Vladimir K. Michaelis, Michael T. Colvin, Ivan Hung, Peter L. Gor’kov, Timothy A. Cross, Zhehong Gan and Robert G. Griffin



Journal of the American Chemical Society
DOI: 10.1021/jacs.7b08989




Source: Journal of the American Chemical Society
0 Replies | 17 Views
Discovery puts the brakes on HIV's ability to infect | EurekAlert ... - EurekAlert (press release)
Dec 01, 2017 - 8:23 AM - by nmrlearner
nmrlearner's Avatar
EurekAlert (press release)


Discovery puts the brakes on HIV's ability to infect | EurekAlert ...
EurekAlert (press release)
In a study led by the University of Delaware and the University of Pittsburgh School of Medicine, researchers discovered a 'brake' that interferes with HIV's development into an infectious agent. This mechanism prevents the capsid -- the protein shell ...

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Discovery puts the brakes on HIV's ability to infect |... [Read More]
0 Replies | 23 Views
Fluorine pharma: Quality control by NMR
Dec 01, 2017 - 8:23 AM - by nmrlearner
nmrlearner's Avatar Fluorine pharma: Quality control by NMR

Routine analysis and quality control of fluorine-containing pharmaceuticals could now be possible with the application of the relatively simple and straightforward technique of fluorine-19 nuclear magnetic resonance (NMR) spectroscopy, according to researchers in Kenya and Germany.

Read the rest at Spectroscopynow.com
0 Replies | 37 Views
Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins
Nov 30, 2017 - 5:01 PM - by nmrlearner
nmrlearner's Avatar Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins

Abstract

Protein structure determination using NMR is dependent on experimentally acquired distance restraints. Often, however, an insufficient number of these restraints are available for determining a proteinâ??s correct fold, much less its detailed three-dimensional structure. In consideration of this problem, we propose a simple means to acquire supplemental structural restraints from protein surface accessibilities using solvent saturation transfer to proteins (SSTP), based on the principles of paramagnetic chemical-exchange saturation transfer. Here, we demonstrate the utility of SSTP in structure calculations of two proteins, TSG101 and ubiquitin. The observed SSTP was found to be directly proportional to solvent accessibility. Since SSTP does not involve the direct excitation of water, which compromises the analysis of protein protons entangled in the breadth of the water resonance, it has an advantage over conventional water-based magnetization transfers. Inclusion of structural restraints derived from SSTP improved both the precision and accuracy of the final protein structures in comparison to those determined by traditional approaches, when using minimal amounts of additional structural data. Furthermore, we show that SSTP can detect weak proteinâ??protein interactions which are unobservable by chemical shift perturbations.



Source: Journal of Biomolecular NMR
0 Replies | 17 Views
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