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Issue 18, 2016
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The removal of disulfide bonds in amylin oligomers leads to the conformational change of the ‘native’ amylin oligomers

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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.

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

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Publication details

The article was received on 22 Feb 2016, accepted on 08 Apr 2016 and first published on 13 Apr 2016


Article type: Communication
DOI: 10.1039/C6CP01196A
Phys. Chem. Chem. Phys., 2016,18, 12438-12442
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    The removal of disulfide bonds in amylin oligomers leads to the conformational change of the ‘native’ amylin oligomers

    V. Wineman-Fisher, L. Tudorachi, E. Nissim and Y. Miller, Phys. Chem. Chem. Phys., 2016, 18, 12438
    DOI: 10.1039/C6CP01196A

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