A Fluorescent Probe with Improved Water SolubilityPermits the Analysis of Protein S-DepalmitoylationActivity in Live Cells
A Fluorescent Probe with Improved Water SolubilityPermits the Analysis of Protein S-DepalmitoylationActivity in Live Cells
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00835/20171018/images/medium/bi-2017-00835x_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00835
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10-19-2017 08:03 AM
Researchers Develop Improved Method for Modeling Protein Complexes via Crosslinking MS - GenomeWeb
Researchers Develop Improved Method for Modeling Protein Complexes via Crosslinking MS - GenomeWeb
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Researchers Develop Improved Method for Modeling Protein Complexes via Crosslinking MS
GenomeWeb
Pasteur Institute researcher Michael Nilges, senior author on the paper, previously tackled a similar problem with using NMR data for elucidating the structures of small proteins, and, Beck said, here Nilges and his co-authors adopted that approach to ...
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04-30-2016 09:26 AM
[NMR paper] Analysis of the interface variability in NMR structure ensembles of protein-protein complexes.
Analysis of the interface variability in NMR structure ensembles of protein-protein complexes.
Related Articles Analysis of the interface variability in NMR structure ensembles of protein-protein complexes.
J Struct Biol. 2016 Mar 8;
Authors: Calvanese L, D'Auria G, Vangone A, Falcigno L, Oliva R
Abstract
NMR structures consist in ensembles of conformers, all satisfying the experimental restraints, which exhibit a certain degree of structural variability. We analyzed here the interface in NMR ensembles of protein-protein...
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03-13-2016 04:25 PM
Analysis of the interface variability in NMR structure ensembles of protein-protein complexes
Analysis of the interface variability in NMR structure ensembles of protein-protein complexes
Publication date: Available online 9 March 2016
Source:Journal of Structural Biology</br>
Author(s): Luisa Calvanese, Gabriella D’Auria, Anna Vangone, Lucia Falcigno, Romina Oliva</br>
NMR structures consist in ensembles of conformers, all satisfying the experimental restraints, which exhibit a certain degree of structural variability. We analyzed here the interface in NMR ensembles of protein-protein heterodimeric complexes and found it to span a wide range of...
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03-09-2016 06:23 AM
[NMR paper] Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements.
Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements.
Related Articles Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements.
Methods Enzymol. 2015;558:333-362
Authors: Hennig J, Warner LR, Simon B, Geerlof A, Mackereth CD, Sattler M
Abstract
Biological activity in the cell is predominantly mediated by large multiprotein and protein-nucleic acid complexes that act together to ensure functional fidelity. Nuclear magnetic resonance...
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06-13-2015 11:09 PM
[NMR paper] Rapid analysis of large protein-protein complexes using NMR-derived orientational con
Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein.
Related Articles Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein.
J Mol Biol. 2004 Nov 5;343(5):1379-89
Authors: Jain NU, Wyckoff TJ, Raetz CR, Prestegard JH
Characterization of protein-protein interactions that are critical to the specific function of many biological systems has become a primary...
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11-24-2010 10:03 PM
[NMR paper] 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes
31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Related Articles 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Eur J Biochem. 2000 Feb;267(4):1223-9
Authors: Castagné C, Murphy EC, Gronenborn AM, Delepierre M
Complexes of the HMG box protein SRY with two duplexes of 8 and 14 base pairs have been studied by 31P NMR and complete assignment of all phosphorus signals of the bound DNA duplexes are presented. While for the free DNA, all 31P signals display limited...
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11-18-2010 09:15 PM
NMR and Small Angle Scattering-based structural analysis of protein complexes in solu
NMR and Small Angle Scattering-based structural analysis of protein complexes in solution.
Related Articles NMR and Small Angle Scattering-based structural analysis of protein complexes in solution.
J Struct Biol. 2010 Nov 10;
Authors: Madl T, Gabel F, Sattler M
Structural analysis of multi-domain protein complexes is a key challenge in current biology and a prerequisite for understanding the molecular basis of essential cellular processes. The use of solution techniques is important for characterizing the quaternary arrangements and dynamics of...
Improved Analysis of RNA Localization by SpatiallyRestricted Oxidation of RNA–Protein Complexes
Linear Mode
