Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos
Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos
[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
[NMR paper] Toward optimal-resolution NMR of intrinsically disordered proteins.
Toward optimal-resolution NMR of intrinsically disordered proteins.
Related Articles Toward optimal-resolution NMR of intrinsically disordered proteins.
J Magn Reson. 2014 Apr;241:41-52
Authors: Nová?ek J, Zídek L, Sklená? V
Abstract
Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their...
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03-25-2014 11:49 AM
[NMR paper] Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Molecules. 2013;18(9):10802-28
Authors: Kosol S, Contreras-Martos S, Cedeńo C, Tompa P
Abstract
Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and intrinsically disordered...
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09-07-2013 09:54 PM
[NMR paper] Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Apr 29;
Authors: Scanu S, Förster J, Ullmann GM, Ubbink M
Abstract
Protein complex formation is thought to be at least a two-step process, in which the active complex is preceded by the formation of an encounter complex....
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05-01-2013 11:46 AM
Intrinsically disordered proteins - PhysicsToday.org
Intrinsically disordered proteins - PhysicsToday.org
<img alt="" height="1" width="1" />
Intrinsically disordered proteins
PhysicsToday.org
Indeed, much of the community's understanding of protein function rests on our ability to deduce those structures by such methods as x-ray crystallography and nuclear magnetic resonance (NMR). The immense success and explanatory power of the ...
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08-01-2012 09:35 PM
Quantitative Analysisof Multisite Protein–LigandInteractions by NMR: Binding of Intrinsically Disordered p53 TransactivationSubdomains with the TAZ2 Domain of CBP
Quantitative Analysisof Multisite Protein–LigandInteractions by NMR: Binding of Intrinsically Disordered p53 TransactivationSubdomains with the TAZ2 Domain of CBP
Munehito Arai, Josephine C. Ferreon and Peter E. Wright
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209936u/aop/images/medium/ja-2011-09936u_0012.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209936u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ak4BxkITHl8
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[NMR paper] Characterization of tertiary interactions in a folded protein by NMR methods: studies
Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
Related Articles Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
Biochemistry. 1992 Sep 15;31(36):8587-96
Authors: Abildgaard F, Jørgensen AM, Led JJ, Christensen T, Jensen EB, Junker F, Dalbøge H
The pH-induced conformational changes in human growth hormone (hGH) have been studied, using a new...
Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos
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