Abstract
The α-helical structure of the N-terminus of the 'native' amylin Lys1-Cys7 consists of a disulfide bond between Cys2 and Cys7. The 'native' amylin oligomers demonstrate polymorphic states. Removal of the disulfide bonds in the 'native' amylin oligomers decreases the polymorphism and induces the formation of longer stable cross-β strands in the N-termini.
| Original language | English |
|---|---|
| Pages (from-to) | 12438-12442 |
| Number of pages | 5 |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 18 |
| Issue number | 18 |
| DOIs | |
| State | Published - 14 May 2016 |
| Externally published | Yes |
Bibliographical note
Publisher Copyright:© 2016 the Owner Societies.
Funding
This research was supported by the Israel Science Foundation (grant No. 532/15) and partly by the FP7-PEOPLE-2011-CIG, research grant No. 303741. All simulations were performed using the high-performance computational facilities of the Miller Lab in the BGU HPC computational center. The support of the BGU HPC computational center staff is greatly appreciated.
| Funders | Funder number |
|---|---|
| Israel Science Foundation | 532/15, 303741, FP7-PEOPLE-2011-CIG |