학술논문

Self-assembly of flexible [beta]-strands into immobile amyloid-like [beta]-sheets in membranes as revealed by solid-state [19 sup]F NMR
Document Type
Report
Source
Journal of the American Chemical Society. April 18, 2012, Vol. 134 Issue 15, 6512-6515
Subject
Structure
Research
Analysis
Amyloid beta-protein -- Structure
Amyloid beta-protein -- Research
Lipid membranes -- Research
Peptide bonds -- Analysis
Protein conformation -- Research
Proteins -- Conformation
Proteins -- Research
Language
English
ISSN
0002-7863
Abstract
The solid-state [19 sup]F NMR technique is employed for examining the mechanisms involved in the self-assembly of the flexible [beta]-strands into immobile amyloid-like [beta]-sheets in membranes. The approach is shown to be extremely beneficial for the examining the membrane-induced amyloid formation of many other, clinically relevant peptide systems.