期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 20, 期 2, 页码 187-195出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2009.12.017
关键词
-
资金
- National Institutes of Health [GM076688-08]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM076688] Funding Source: NIH RePORTER
Identifying the principles that describe the formation of protein oligomers and fibrils with distinct morphologies is a daunting problem. Here we summarize general principles of oligomer formation gleaned from molecular dynamics simulations of A beta-peptides. The spectra of high free energy structures sampled by the monomer provide insights into the plausible fibril structures, providing a rationale for the 'strain phenomenon.' Heterogeneous growth dynamics of small oligomers of A beta(16-22), whose lowest free energy structures are like nematic droplets, can be broadly described using a two-stage dock-lock mechanism. In the growth process, water is found to play various roles depending on the oligomer size, and peptide length, and sequence. Water may be an explicit element of fibril structure linked to various fibril morphologies.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据