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

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

14 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 - 2016
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2016 the Owner Societies.

Access to Document

10.1039/c6cp01196a

Cite this

@article{8f6674d6262446abad7d26350215ebb7,

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",

note = "Publisher Copyright: {\textcopyright} 2016 the Owner Societies.",

year = "2016",

doi = "10.1039/c6cp01196a",

language = "אנגלית",

volume = "18",

pages = "12438--12442",

journal = "Physical Chemistry Chemical Physics",

issn = "1463-9076",

publisher = "Royal Society of Chemistry",

number = "18",

}

TY - JOUR

T1 - The removal of disulfide bonds in amylin oligomers leads to the conformational change of the 'native' amylin oligomers

AU - Wineman-Fisher, Vered

AU - Tudorachi, Lucia

AU - Nissim, Einav

AU - Miller, Yifat

PY - 2016

Y1 - 2016

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.

UR - http://www.scopus.com/inward/record.url?scp=84973551322&partnerID=8YFLogxK

U2 - 10.1039/c6cp01196a

DO - 10.1039/c6cp01196a

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 27109452

AN - SCOPUS:84973551322

SN - 1463-9076

VL - 18

SP - 12438

EP - 12442

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

IS - 18

ER -

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

Abstract

Bibliographical note

Access to Document

Other files and links

Fingerprint

Cite this