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

Ben-Gurion University of the Negev

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

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 - 14 May 2016

All Science Journal Classification (ASJC) codes

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1039/c6cp01196a

Cite this

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title = "The removal of disulfide bonds in amylin oligomers leads to the conformational change of the 'native' amylin oligomers",

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.",

author = "Vered Wineman-Fisher and Lucia Tudorachi and Einav Nissim and Yifat Miller",

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year = "2016",

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doi = "10.1039/c6cp01196a",

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AU - Tudorachi, Lucia

AU - Nissim, Einav

AU - Miller, Yifat

PY - 2016/5/14

Y1 - 2016/5/14

N2 - 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.

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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M3 - مقالة

C2 - 27109452

SN - 1463-9076

VL - 18

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EP - 12442

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

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ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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