期刊
BIOCHEMISTRY
卷 47, 期 38, 页码 10018-10026出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi801081c
关键词
-
资金
- U. Chicago Argonne, LLC [DE-AC02-06CH11357]
- Apkarian Electron Microscopy Facility
- Emory University
- [DOE ER15377]
- [NSF-CHE 0404677]
- [NSF-CHE 0739189]
Amino acid cross-strand pairing interactions along a P-sheet surface have been implicated in protein P-structural assembly and stability, yet the relative contributions have been difficult to evaluate directly. Here we develop the central core sequence of the A beta peptide associated with Alzheimer's disease, A beta(16-22), as an experimental system for evaluating these interactions. The peptide allows for internal comparisons between electrostatic and steric interactions within the P-sheet and an evaluation of these cross-strand pair contributions to beta-sheet registry. A morphological transition from fibers to hollow nanotubes arises from changes in beta-sheet surface complementarity and provides a convenient indicator of the beta-strand strand registry. The intrinsic beta-sequence and pair correlations are critical to regulate secondary assembly. These studies provide evidence for a critical desolvation step that is not present in most models of the nucleation-dependent pathway for amyloid assembly.
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