Unique Inversion Events of Residues around the Backbone in the Turn Domain of β-Arches in Amylin Fibrils

被引：2
作者：
Atsmon-Raz, Yoav [1 ,2 ]
Wineman-Fisher, Vered [3 ]
Baram, Michal [1 ,2 ]
Miller, Yifat [1 ,2 ]
机构：
[1] Ben Gurion Univ Negev, Dept Chem, IL-84105 Beer Sheva, Israel
[2] Ben Gurion Univ Negev, Ilse Katz Inst Nanoscale Sci & Technol, IL-84105 Beer Sheva, Israel
[3] Univ S Florida, Dept Cell Biol Microbiol & Mol Biol, Tampa, FL 33620 USA
来源：
ACS CHEMICAL NEUROSCIENCE | 2019年 / 10卷 / 03期
基金：
以色列科学基金会;
关键词：
Amyloid; self-assembly; peptide-plane in proteins; polymorphism; structural interconversion; DIABETES-MELLITUS; OLIGOMERS; DISEASE; RISK;
D O I：
10.1021/acschemneuro.8b00554
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Orientational inversion events of residues along the turn domains of amylin fibrils have been detected. This exceptional phenomenon has been observed in isolated amylin fibrils and in the cross -seeding amylin-A beta and amylin-NAC fibrils. These new findings provide new avenues for detection of side chain flipping and side chain inversion events in turn domains and loops of various proteins.
引用
收藏
页码：1209 / 1213
页数：9
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