Investigation of the Binding Interaction of FattyAcids with Human G Protein-Coupled Receptor 40 Using a Site-SpecificFluorescence Probe by Flow Cytometry
Investigation of the Binding Interaction of FattyAcids with Human G Protein-Coupled Receptor 40 Using a Site-SpecificFluorescence Probe by Flow Cytometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00079/20160317/images/medium/bi-2016-00079r_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00079
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03-18-2016 04:29 AM
[NMR paper] NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment.
NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment.
NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment.
J Am Chem Soc. 2016 Mar 4;
Authors: Orts J, Wälti MA, Marsh M, Vera L, Gossert AD, Güntert P, Riek R
Abstract
Molecular replacement in X-ray crystallography is the prime method for establishing structure-activity relationships of pharmaceutically relevant molecules. Such an approach is not...
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03-05-2016 11:21 AM
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
J Am Chem Soc. 2010 Dec 16;
Authors: Gossert AD, Hiller S, Ferna?ndez C
The detection and structural characterization of protein-ligand interactions by solution NMR is central to functional biology research as well as to drug discovery. Here we present a robust and highly automated procedure for obtaining the resonance assignments necessary for studies of such...
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12-18-2010 12:00 PM
A novel strategy for NMR resonance assignment and protein structure determination
A novel strategy for NMR resonance assignment and protein structure determination
Abstract The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR data have posed challenges for the routine and automated structure determination of small to medium sized proteins; (1) spectral resolution â?? especially of crowded nuclear Overhauser effect spectroscopy (NOESY) spectra, and (2) the reliance on a...
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12-18-2010 01:31 AM
A novel strategy for NMR resonance assignment and protein structure determination.
A novel strategy for NMR resonance assignment and protein structure determination.
A novel strategy for NMR resonance assignment and protein structure determination.
J Biomol NMR. 2010 Dec 14;
Authors: Lemak A, Gutmanas A, Chitayat S, Karra M, Farès C, Sunnerhagen M, Arrowsmith CH
The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR data have posed...
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12-17-2010 11:23 AM
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies
Alvar D. Gossert, Sebastian Hiller and Ce?sar Ferna?ndez
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108383x/aop/images/medium/ja-2010-08383x_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108383x
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12-17-2010 12:50 AM
[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in
NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
Related Articles NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
J Biomol NMR. 2002 Jun;23(2):151-2
Authors: Espejo F, Green M, Preece NE, Assa-Munt N
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11-24-2010 08:49 PM
Robust structure-based resonance assignment for functional protein studies by NMR
Abstract High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that are not based on J-coupling and for which connections between residues are not limited by through bonds magnetization transfer efficiency. We present here a robust structure-based assignment...