All-atom structure ensembles of islet amyloid polypeptides determined by enhanced sampling and experiment data restraints

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成果类型：

期刊论文

作者：

Su, Xinyue;Wang, Ke;Liu, Na;Chen, Jiawen;Li, Yong*;...

通讯作者：

Li, Yong;Duan, Mojie

作者机构：

[Liu, Na; Su, Xinyue; Wang, Ke; Chen, Jiawen; Duan, Mojie] Chinese Acad Sci, CAS Key Lab Magnet Resonance Biol Syst, State Key Lab Magnet Resonance & Atom & Mol Phys, Natl Ctr Magnet Resonance Wuhan,Wuhan Inst Phys &, Wuhan, Hubei, Peoples R China.

[Su, Xinyue; Li, Yong] Cent China Normal Univ, Dept Phys, 152 Luoyu Rd, Wuhan 430079, Hubei, Peoples R China.

[Liu, Na; Wang, Ke] Univ Chinese Acad Sci, Dept Chem, Beijing, Peoples R China.

[Duan, Mojie] Chinese Acad Sci, Wuhan Inst Phys & Math, 30 Xiao Hong Shan West, Wuhan 430071, Hubei, Peoples R China.

通讯机构：

[Li, Yong; Duan, Mojie] C

Cent China Normal Univ, Dept Phys, 152 Luoyu Rd, Wuhan 430079, Hubei, Peoples R China.

Chinese Acad Sci, Wuhan Inst Phys & Math, 30 Xiao Hong Shan West, Wuhan 430071, Hubei, Peoples R China.

语种：

英文

关键词：

aggregation;chemical shift restraint;islet amylod polypeptide;metadynamics

期刊：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

ISSN：

0887-3585

年：

2019

卷：

期：

页码：

541-550

DOI：

10.1002/prot.25677

基金类别：

National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21773298, 21403291]

机构署名：

本校为通讯机构

院系归属：

物理科学与技术学院

摘要：

Exploring the accurate structure ensembles are critical to understand the functions of intrinsically disordered proteins (IDPs). As a well-known IDP, islet amyloid polypeptide (IAPP) plays important roles in the development of human type II diabetes (T2D). The toxicity of human IAPP (hIAPP) is induced by the amyloidosis of the peptide, however, its aggregation mechanism remains ambiguous. The characterization of structure ensemble of hIAPP, as well as the differences between hIAPP and its non-amyloidogenic homologous such as rat IAPP (rIAPP), would greatly help to illuminate the amyloidosis me...

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All-atom structure ensembles of islet amyloid polypeptides determined by enhanced sampling and experiment data restraints

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