Guanghong Wei

TL;DR: In this paper, the authors review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease, Parkinson's disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research.

TL;DR: This review highlights recent studies that illustrate functional adjustment of protein conformational ensembles in the crowded cellular environment and focuses on the role of the ensemble in recognition of small- and macro-molecules and emerging concepts of protein dynamics in enzyme catalysis.

TL;DR: This study provides, for the first time, the self-assembly mechanism and the molecular organization of FF dipeptide nanostructures.

TL;DR: This study uses large-scale molecular dynamics simulations to study the interaction between several proteins (WW domains) and carbon nanotubes (one form of hydrophobic nanoparticles) and finds that the carbon Nanotube can plug into the hydrophilic core of proteins to form stable complexes.

TL;DR: Investigating the conformations of Aβ(16-22) octamers in the absence and presence of a single-walled carbon nanotube (SWCNT) by performing extensive all-atom replica exchange molecular-dynamics simulations in explicit solvent provides evidence that SWCNT is likely to inhibit Aβ (16- 22) and full-length Aβ fibrillation.