Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 15;
Authors: Binolfi A, Valiente-Gabioud AA, Duran R, Zweckstetter M, Griesinger C, Fernandez CO
The aggregation of ?-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS.
PMID: 21158432 [PubMed - as supplied by publisher]
Exploring NMR ensembles of calcium binding proteins: perspectives to design ... - 7thSpace Interactive (press release)
Exploring NMR ensembles of calcium binding proteins: perspectives to design ... - 7thSpace Interactive (press release)
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Exploring NMR ensembles of calcium binding proteins: perspectives to design ...
7thSpace Interactive (press release)
We employed several scoring methods in order to find the best protein conformations. Our results show that docking on NMR structures of calmodulin and centrin can be very helpful to take into account conformational changes occurring at protein-protein ...
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05-13-2011 07:41 AM
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Feb 1;17(5):1519-1528
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute...
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Jan 5;
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute 2 protein of...
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01-06-2011 11:21 AM
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy
Andres Binolfi, Ariel A. Valiente-Gabioud, Rosario Duran, Markus Zweckstetter, Christian Griesinger and Claudio O. Fernandez
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107842f/aop/images/medium/ja-2010-07842f_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107842f
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/b4TqLrO3oG4
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12-16-2010 12:37 AM
[NMR paper] Transient complexes of redox proteins: structural and dynamic details from NMR studie
Transient complexes of redox proteins: structural and dynamic details from NMR studies.
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J Mol Recognit. 2004 Nov-Dec;17(6):524-39
Authors: Prudêncio M, Ubbink M
Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Protein-protein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Two-dimensional NMR spectroscopy has been applied to many redox protein...
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11-24-2010 10:03 PM
[NMR paper] Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd
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Biochemistry. 2000 Jun 13;39(23):6751-5
Authors: Matysik J, Alia A, Nachtegaal G, van Gorkom HJ, Hoff AJ, de Groot HJ
Calcium (Ca(2+)) is an essential cofactor for photosynthetic oxygen evolution. Although the involvement of Ca(2+) at the oxidizing side of photosystem II of plants has been known for a long time, its ligand interactions and mode of...
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11-18-2010 09:15 PM
[NMR paper] Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with
Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with the aid of spin-labeled oligonucleotides in combination with 1H-NMR.
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Biochemistry. 1993 Sep 14;32(36):9407-16
Authors: Folkers PJ, van Duynhoven JP, van Lieshout HT, Harmsen BJ, van Boom JH, Tesser GI, Konings RN, Hilbers CW
The DNA binding domain of the single-stranded DNA binding protein...
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
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