Ice-binding proteins (IBPs) are unique molecules that bind to and are active on the interface
between two phases of water: ice and liquid water. This property allows them to affect ice …

Antifreeze proteins (AFPs) are of much interest for their ability to inhibit ice growth at low
concentrations. In this work, we present a genetic algorithm for the in silico design of AFP …

We investigate the microscopic pathway of spontaneous crystallization in the ST2 model of
water under deeply supercooled conditions via unbiased classical molecular dynamics …

In the theory of solidification, the kinetic coefficient multiplies the local supercooling to give
the solid–liquid interface velocity. The same coefficient should drive interface migration at …

Some of the most potent antifreeze proteins (AFPs) are approximately rigid helical structures
that bind with one side in contact with the ice surface at specific orientations. These AFPs …

Recognition and binding of ice by proteins, crystals, and other surfaces is key for their
control of the nucleation and growth of ice. Docking is the state-of-the-art computational …

Recrystallization of ice is a natural phenomenon that causes adverse effects in
cryopreservation, agriculture, and in frozen food industry. It has long been recognized that …

Interfaces between hexagonal ice and its vapor, liquid water, and aqueous solutions are all
of central importance to life on earth. Despite its importance, much remains unknown about …

Antifreeze proteins (AFPs) are biopolymers capable of interfering with ice growth. Their
antifreeze action is commonly understood considering that the AFPs, by pinning the ice …

Antifreeze proteins (AFPs) bind to the ice–water surface and prevent ice growth at
temperatures below 0° C through a Gibbs–Thomson effect. Each adsorbed AFP creates a …