| Title |
The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218–289): a solid-state NMR study
|
|---|---|
| Published in |
Journal of Biomolecular NMR, November 2017
|
| DOI | 10.1007/s10858-017-0148-z |
| Pubmed ID | |
| Authors |
Chandrakala Gowda, Giorgia Zandomeneghi, Herbert Zimmermann, Anne K. Schütz, Anja Böckmann, Matthias Ernst, Beat H. Meier |
| 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 (13)C labeling of CR and on the analysis of the two-dimensional magic-angle spinning tensor-correlation spectrum of (13)C2-CR. We determined the torsion angle ϕ to be 19°. |
Mendeley readers
The data shown below were compiled from readership statistics for 19 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 19 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 5 | 26% |
| Researcher | 3 | 16% |
| Professor | 2 | 11% |
| Other | 1 | 5% |
| Student > Bachelor | 1 | 5% |
| Other | 3 | 16% |
| Unknown | 4 | 21% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 5 | 26% |
| Chemistry | 5 | 26% |
| Immunology and Microbiology | 1 | 5% |
| Unspecified | 1 | 5% |
| Neuroscience | 1 | 5% |
| Other | 1 | 5% |
| Unknown | 5 | 26% |