Amyloid and amyloid-like fibrils are self-assembling protein nanostructures, of interest for
their robust material properties and inherent biological compatibility as well as their putative …

Directing self‐assembly processes out‐of‐equilibrium to yield kinetically trapped materials
with well‐defined dimensions remains a considerable challenge. Kinetically controlled …

The ordered assembly of amyloidogenic proteins causes a wide spectrum of common
neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. These …

We propose a kinetic model for the self-aggregation by amyloid proteins. By extending
several well-known models for protein aggregation, the time evolution of aggregate …

Human amyloids and plaques uncovered post mortem are highly heterogeneous in structure
and composition, yet literature concerning the heteroaggregation of amyloid proteins is …

In small volumes, the kinetics of filamentous protein self-assembly is expected to show
significant variability, arising from intrinsic molecular noise. This is not accounted for in …

The partial equilibrium approximation (PEA) and the quasi-steady-state approximation
(QSSA) are two classical methods for reducing complex macroscopic chemical reactions …

The formation of elongated supra-molecular structures from protein building blocks
generates functional intracellular filaments, but this process is also at the heart of many …

Due to the intrinsic complexity and nonlinearity of chemical reactions, direct applications of
traditional machine learning algorithms may face many difficulties. In this study, through two …

Protein aggregation is of great importance in biology, eg, in amyloid fibrillation. The
aggregation processes that occur at the cellular scale must be highly stochastic in nature …