English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
 Local TagsRelease HistoryDetailsSummary
  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.

Item is

 

show all hide all

Basic

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

Files

show Files
hide Files
:
JBiomolNMR_69_2017_207.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
JBiomolNMR_69_2017_207.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
JBiomolNMR_69_2017_207_Suppl.pdf (Supplementary material), 451KB
 
File Permalink:
-
Name:
JBiomolNMR_69_2017_207_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
https://link.springer.com/content/pdf/10.1007%2Fs10858-017-0148-z.pdf (Any fulltext)
Description:
-
OA-Status:
Locator:
https://static-content.springer.com/esm/art%3A10.1007%2Fs10858-017-0148-z/MediaObjects/10858_2017_148_MOESM1_ESM.pdf (Supplementary material)
Description:
-
OA-Status:
Locator:
https://doi.org/10.1007/s10858-017-0148-z (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 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              

Content

show
hide
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°.

Details

show
hide
Language(s): eng - English
 Dates: 2017-07-302017-10-212017-11-012017-12
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s10858-017-0148-z
URI: https://www.ncbi.nlm.nih.gov/pubmed/29094285
URI: https://www.ncbi.nlm.nih.gov/m/pubmed/29094285/
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biomolecular NMR
  Abbreviation : J. Biomol. NMR
Source Genre: Journal
 Creator(s):
Affiliations:
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: https://pure.mpg.de/cone/journals/resource/954925566734