[ASAP] Single-Molecule Tracking Approaches to Protein Synthesis Kinetics in Living Cells
Single-Molecule Tracking Approaches to Protein Synthesis Kinetics in Living Cells
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00917/20181114/images/medium/bi-2018-009172_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00917
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11-25-2018 06:02 AM
[ASAP] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00195/20180430/images/medium/bi-2018-001959_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00195
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05-01-2018 10:57 PM
Label-free NMR-based dissociation kinetics determination
Label-free NMR-based dissociation kinetics determination
Abstract
Understanding the dissociation of molecules is the basis to modulate interactions of biomedical interest. Optimizing drugs for dissociation rates is found to be important for their efficacy, selectivity, and safety. Here, we show an application of the high-power relaxation dispersion (RD) method to the determination of the dissociation rates of weak binding ligands from receptors. The experiment probes proton RD on the ligand and, therefore, avoids the need for any isotopic labeling....
nmrlearner
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11-16-2017 10:50 AM
[NMR paper] Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
Related Articles Unraveling the conformational landscape of ligand binding to Glucose/Galactose-binding protein by paramagnetic NMR and MD simulations.
ACS Chem Biol. 2016 May 24;
Authors: Unione L, Ortega G, Mallagaray A, Corzana F, Perez-Castells J, Canales A, Jimenez-Barbero J, Millet O
Abstract
Protein dynamics related to function can be nowadays structurally well characterized (i. e....
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05-25-2016 02:33 PM
Superconducting Magnets Used to Observe Proteins, Atom-by-Atom - Azom.com
Superconducting Magnets Used to Observe Proteins, Atom-by-Atom - Azom.com
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Superconducting Magnets Used to Observe Proteins, Atom-by-Atom
Azom.com
â??This is a very specialized facility,â?? says Stanley Opella, professor of chemistry and biochemistry and director of the Center for NMR Spectroscopy and Imaging of Proteins, the organization that operates this building. The purpose of the facility is to ...
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10-27-2012 03:04 AM
Accuracy and precision of proteinâ??ligand interaction kinetics determined from chemical shift titrations
Accuracy and precision of proteinâ??ligand interaction kinetics determined from chemical shift titrations
Abstract NMR-monitored chemical shift titrations for the study of weak proteinâ??ligand interactions represent a rich source of information regarding thermodynamic parameters such as dissociation constants (K D ) in the micro- to millimolar range, populations for the free and ligand-bound states, and the kinetics of interconversion between states, which are typically within the fast exchange regime on the NMR timescale. We recently developed two chemical shift titration methods...
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10-24-2012 10:28 PM
Increased precision for analysis of proteinâ??ligand dissociation constants determined from chemical shift titrations
Increased precision for analysis of proteinâ??ligand dissociation constants determined from chemical shift titrations
Abstract NMR is ideally suited for the analysis of proteinâ??protein and protein ligand interactions with dissociation constants ranging from ~2 ÎĽM to ~1 mM, and with kinetics in the fast exchange regime on the NMR timescale. For the determination of dissociation constants (K D ) of 1:1 proteinâ??protein or proteinâ??ligand interactions using NMR, the protein and ligand concentrations must necessarily be similar in magnitude to the K D , and nonlinear least squares...
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05-01-2012 07:06 AM
[NMR paper] NMR methods for the determination of protein-ligand dissociation constants.
NMR methods for the determination of protein-ligand dissociation constants.
Related Articles NMR methods for the determination of protein-ligand dissociation constants.
Curr Top Med Chem. 2003;3(1):39-53
Authors: Fielding L
This article is a review with 83 references of the application of NMR to the measurement of the dissociation constants of protein-ligand complexes. After briefly discussing some general concepts of molecular stability, the text turns to consider which NMR parameters are reporters of complex formation. The available data...
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[ASAP] Kinetics of Ligand–Protein Dissociation from All-Atom Simulations: Are We There Yet?
Linear Mode
