Related Experiment Video
Updated: Jan 28, 2026

Three-Dimensional Shape Modeling and Analysis of Brain Structures
Published on: November 14, 2019
A DFT-Assisted Topological Analysis of Four Polymorphic, S-Shaped Aβ42 Fibril Structures
Alejandro R Foley1, Jevgenij A Raskatov1
1Department of Chemistry and Biochemistry, University of California Santa Cruz, Physical Science Building 356, 1156 High Street, Santa Cruz, CA, 95064, USA.
Abstract:
Amyloid β 42 (Aβ42) is an inherently disordered peptide, whose toxic actions are believed to play important roles in the etiology of Alzheimer's disease. Four fibril structures of the peptide that display broadly similar characteristics were recently published, but a systematic comparison of these structures is lacking. In this paper, a topological framework was created to enable such understanding and produced new insights into subtle structural elements that underlie the overall structural diversity. A DFT-based analysis illuminated some of the energetic differences that arise as a consequence.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid Fibrils
Relation of DFT to z-Transform
To understand how the DFT works, it's helpful to consider the z-transform, which is a method for representing discrete sequences in the complex frequency domain. The z-transform involves summing the...
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
VSEPR Theory and the Basic Shapes
Molecular Shapes
Two regions of electron density in a diatomic...

