作者
Rozita Laghaei, Normand Mousseau, Guanghong Wei
发表日期
2010/5/27
期刊
The journal of physical chemistry B
卷号
114
期号
20
页码范围
7071-7077
出版商
American Chemical Society
简介
The human Islet amyloid polypeptide (hIAPP or amylin) is a 37-residue peptide hormone that is normally cosecreted with insulin by the pancreatic β-cells. In patients with type 2 diabetes, hIAPP deposits as amyloid fibrils in the extracellular spaces of the pancreatic islets. Recent experimental studies show that the intramolecular disulfide bond between Cys2 and Cys7 plays a central role in the process of fibril formation. However, the effect of the disulfide bond on the intrinsic structural properties of monomeric hIAPP is yet to be determined. In this study, we characterize the atomic structure and the thermodynamics of full-length hIAPP in the presence and absence of a disulfide bond using extensive combined Hamiltonian and temperature replica exchange molecular dynamics simulations (HT-REMD) with a coarse grained protein force field. Our simulations show that HT-REMD is more efficient in sampling than …
学术搜索中的文章
R Laghaei, N Mousseau, G Wei - The journal of physical chemistry B, 2010