Related ArticlesCa(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Biochim Biophys Acta. 2013 Dec 4;
Authors: Zhang Z, Dai C, Bai J, Xu G, Liu M, Li C
Abstract
?-synuclein is involved in Parkinson's disease and its interaction with cell membrane is crucial to its pathological and physiological functions. Membrane properties, such as curvature, lipid composition have been shown to affect the interactions by various techniques, but ion effects on ?-synuclein membrane interactions remain elusive. Ca(2+) dynamic fluctuation in neurons plays important roles in the onset of Parkinson's disease and its influx is considered as one of the reasons to cause cell death. Using solution NMR spectroscopy, here we show that Ca(2+) can modulate ?-synuclein membrane interactions through competitive binding to anionic lipids, resulting in dissociation of ?-synuclein from membranes. These results suggest a negative modulatory effect of Ca(2+) on membrane mediated normal function of ?-synuclein, which may provide a clue, to their dysfunction in neurodegenerative disease.
PMID: 24316000 [PubMed - as supplied by publisher]
Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
Sandra Scanu, Johannes M. Foerster, G. Matthias Ullmann and Marcellus Ubbink
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4015452/aop/images/medium/ja-2013-015452_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4015452
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/I9ARcKlvRs8
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[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
[NMR paper] Perfluoro-tert-butyl-homoserine as a sensitive (19) F NMR reporter for peptide-membrane interactions in solution.
Perfluoro-tert-butyl-homoserine as a sensitive (19) F NMR reporter for peptide-membrane interactions in solution.
Related Articles Perfluoro-tert-butyl-homoserine as a sensitive (19) F NMR reporter for peptide-membrane interactions in solution.
J Pept Sci. 2013 Mar 19;
Authors: Buer BC, Levin BJ, Marsh EN
Abstract
Fluorine ((19) F) NMR is a valuable tool for studying dynamic biological processes. However, increasing the sensitivity of fluorinated reporter molecules is a key to reducing acquisition times and accessing transient...
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Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
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09-30-2011 05:59 AM
[NMR paper] Close encounters of the transient kind: protein interactions in the photosynthetic re
Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy.
Related Articles Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy.
Acc Chem Res. 2003 Oct;36(10):723-30
Authors: Crowley PB, Ubbink M
Plastocyanin and cytochrome c(6) function as electron shuttles between cytochrome f and photosystem I in the photosynthetic redox chain. To transfer electrons the partners form transient complexes, which are...
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11-24-2010 09:16 PM
[NMR paper] Probing the kinetic landscape of transient peptide-protein interactions by use of pep
Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
Related Articles Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
J Am Chem Soc. 2003 Oct 15;125(41):12432-42
Authors: Tolkatchev D, Xu P, Ni F
Protein-ligand interactions may lead to the formation of multiple...
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[NMR paper] Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C
Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Related Articles Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Biochemistry. 2003 Jun 17;42(23):7068-76
Authors: Worrall JA, Reinle W, Bernhardt R, Ubbink M
The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional...
Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
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