Acyl carrier proteins (ACPs) are central to many primary and secondary metabolic pathways. In E. coli fatty acid biosynthesis (FAB), the central ACP, AcpP, transports intermediates to a suite of partner proteins (PP) for iterative modification and elongation. The regulatory protein-protein interactions that occur between AcpP and the PP in FAB are poorly understood due to the dynamic and transient nature of these interactions. Solution-state NMR spectroscopy can reveal information at the atomic...
[NMR paper] Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
PLoS One. 2017;12(9):e0184487
Authors: Delius J, Frank O, Hofmann T
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is well-established in assessing the binding affinity between...
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09-09-2017 06:59 PM
[NMR paper] Peptide-Directed Binding for the Discovery of Modulators of ?-Helix-Mediated Protein–Protein Interactions: Proof-of-Concept Studies with the Apoptosis Regulator Mcl-1
Peptide-Directed Binding for the Discovery of Modulators of ?-Helix-Mediated Protein–Protein Interactions: Proof-of-Concept Studies with the Apoptosis Regulator Mcl-1
Targeting PPIs with small molecules can be challenging owing to large, hydrophobic binding surfaces. Herein, we describe a strategy that exploits selective ?-helical PPIs, transferring these characteristics to small molecules. The proof of concept is demonstrated with the apoptosis regulator Mcl-1, commonly exploited by cancers to avoid cell death. Peptide-directed binding uses few synthetic transformations, requires the...
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07-25-2017 07:46 PM
[NMR paper] Peptide directed binding; a novel approach for the discovery of modulators of alpha-helix mediated protein-protein interactions demonstrated with apoptosis regulating Mcl-1
Peptide directed binding; a novel approach for the discovery of modulators of alpha-helix mediated protein-protein interactions demonstrated with apoptosis regulating Mcl-1
Targeting PPIs with small molecules can be challenging due to large, hydrophobic binding surfaces. Here, we describe a strategy that exploits selective alpha-helical PPIs, transferring these characteristics to small molecules. The proof-of-concept is exemplified with the apoptosis regulator Mcl-1, commonly exploited by cancers to avoid cell death. Peptide directed binding uses few synthetic transformations, requires...
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07-03-2017 02:31 AM
Substrate–Protein Interactions of Type II NADH:QuinoneOxidoreductase from Escherichia coli
Substrate–Protein Interactions of Type II NADH:QuinoneOxidoreductase from Escherichia coli
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00070/20160505/images/medium/bi-2016-00070d_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00070
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/kAUMGMWV_Qs
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[NMR paper] Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Related Articles Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
J Biol Chem. 2014 Aug 13;
Authors: Meneses E, Mittermaier A
Abstract
Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about...
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08-15-2014 12:53 PM
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Chembiochem. 2011 Mar 29;
Authors: Crowley PB, Chow E, Papkovskaia T
Protein science is shifting towards experiments performed under native or native-like conditions. In-cell NMR spectroscopy for instance has the potential to reveal protein structure and dynamics inside cells. However, not all proteins can be studied by this technique. (15) N-labelled...
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[NMR paper] Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by
Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range.
Related Articles Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range.
Biochim Biophys Acta. 2005 Apr-May;1707(2-3):254-8
Authors: Pedersen A, Johansson T, Rydström J, Göran Karlsson B
A pH-titration 2D NMR study of Escherichia coli transhydrogenase domain III with...
Using NMR Titration Experiments to Study E. coli FAS-II- and AcpP-Mediated Protein-Protein Interactions
Linear Mode
