Yifat Miller
Senior Academic
The removal of disulfide bonds in amylin oligomers leads to the conformational change of the 'native' amylin oligomers
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.
| Publication language | English |
| Pages | 12438-12442 |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 18 |
| Issue number | 18 |
| Publication status | Published - 01.01.2016 |
ASJC Scopus subject areas
General Physics and Astronomy
Physical and Theoretical Chemistry
