Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 18, Issue 18, Pages 12438-12442Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6cp01196a
Keywords
-
Funding
- Israel Science Foundation [532/15]
- FP7-PEOPLE-CIG [303741]
Ask authors/readers for more resources
The alpha-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-beta strands in the N-termini.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available