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  The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218–289): a solid-state NMR study

Gowda, C., Zandomeneghi, G., Zimmermann, H., Schütz, A. K., Böckmann, A., Ernst, M., et al. (2017). The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218–289): a solid-state NMR study. Journal of Biomolecular NMR, 69(4), 207-213. doi:10.1007/s10858-017-0148-z.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2349-D Version Permalink: http://hdl.handle.net/21.11116/0000-0000-29AF-E
Genre: Journal Article

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JBiomolNMR_69_2017_207_Suppl.pdf (Supplementary material), 451KB
 
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 Creators:
Gowda, Chandrakala, Author
Zandomeneghi, Giorgia, Author
Zimmermann, Herbert1, Author              
Schütz, Anne K., Author
Böckmann, Anja, Author
Ernst, Matthias, Author
Meier, Beat H., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: MAS; Amyloid fibrils; Congo red; Rotor-synchronized tensor-correlation experiments
 Abstract: We have previously shown that Congo red (CR) binds site specifically to amyloid fibrils formed by HET-s(218–289) with the long axis of the CR molecule almost parallel to the fibril axis. HADDOCK docking studies indicated that CR adopts a roughly planar conformation with the torsion angle ϕ characterizing the relative orientation of the two phenyl rings being a few degrees. In this study, we experimentally determine the torsion angle ϕ at the center of the CR molecule when bound to HET-s(218–289) amyloid fibrils using solid-state NMR tensor-correlation experiments. The method described here relies on the site-specific 13C labeling of CR and on the analysis of the two-dimensional magic-angle spinning tensor-correlation spectrum of 13C2-CR. We determined the torsion angle ϕ to be 19°.

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Language(s): eng - English
 Dates: 2017-07-302017-10-212017-11-012017-12
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: Journal of Biomolecular NMR
  Abbreviation : J. Biomol. NMR
Source Genre: Journal
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Publ. Info: Dordrecht, The Netherlands : Springer Science+Business Media
Pages: - Volume / Issue: 69 (4) Sequence Number: - Start / End Page: 207 - 213 Identifier: ISSN: 0925-2738
CoNE: /journals/resource/954925566734