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

Vered Wineman-Fisher; Lucia Tudorachi; Einav Nissim; Yifat Miller

doi:10.1039/c6cp01196a

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

Vered Wineman-Fisher, Lucia Tudorachi, Einav Nissim, Yifat Miller

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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	https://doi.org/10.1039/c6cp01196a
State	Published - 1 Jan 2016

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1039/c6cp01196a

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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.",

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AU - Miller, Yifat

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AB - 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.

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

Abstract

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