Literature DB >> 27109452

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

Vered Wineman-Fisher1, Lucia Tudorachi, Einav Nissim, Yifat Miller.   

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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Year:  2016        PMID： 27109452     DOI： 10.1039/c6cp01196a

Source DB:  PubMed          Journal:  Phys Chem Chem Phys        ISSN： 1463-9076            Impact factor:   3.676


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