| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10536851 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2012 | 12 Pages |
Abstract
⺠We examine backbone contribution to fibril stability using modified peptides. ⺠The backbone is extremely sensitive to substitutions. ⺠One analogue could elongate fibril seeds, none could fibrillate on their own. ⺠The resulting fibrils display differences in secondary structure and morphology. ⺠Side-chain mutations had little effect on fibrillation kinetics and stability.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Maria Andreasen, Søren B. Nielsen, Tina Mittag, Morten Bjerring, Jakob T. Nielsen, Shuai Zhang, Erik H. Nielsen, Martin Jeppesen, Gunna Christiansen, Flemming Besenbacher, Mingdong Dong, Niels Chr. Nielsen, Troels Skrydstrup, Daniel E. Otzen,