Mechanistic Insights into the Folding Mechanism of Region V in Ice-Binding Protein Secreted by Revealed by Single-Molecule Force Spectroscopy.

The Gram-negative bacteria secrete an ice-binding protein (IBP), which is a vital bacterial adhesin facilitating the adaptation and survival of the bacteria in the harsh Antarctic environment. The C-terminal region of IBP, known as region V (RV), is the first domain to be exported into the Ca-rich extracellular environment and acts as a folding nucleus for the entire adhesin. However, the mechanisms underlying the secretion and folding of RV remain poorly understood.

Dielectric engineering enable to lateral anti-ambipolar MoTeheterojunction.

Atomically two-dimensional (2D) materials have generated widespread interest for novel electronics and optoelectronics. Specially, owing to atomically thin 2D structure, the electronic bandgap of 2D semiconductors can be engineered by manipulating the surrounding dielectric environment. In this work, we develop an effective and controllable approach to manipulate dielectric properties of h-BN through gallium ions (Ga) implantation for the first time.