The removal of disulfide bonds in amylin oligomers leads to the conformational change of the ‘native’ amylin oligomers

文献情報

出版日 2016-04-13

DOI 10.1039/C6CP01196A

インパクトファクター 3.676

著者

Lucia Tudorachi

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要旨

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.

掲載誌

Physical Chemistry Chemical Physics

CiteScore: 5.5

自己引用率: 10.3%

年間論文数: 3036

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