The molecular mechanism behind the ice growth inhibition by antifreeze proteins (AFPs) is
yet to be understood completely. Also, what physical parameters differentiate between the …

The existence of two structural forms in liquid water has been a point of discussion for a long
time. A phase transition between these two forms of liquid water has been proposed based …

Bacteria containing ice-nucleating proteins (INPs) evolved in nature to nucleate ice at the
high sub-zero ambiance. The ability of the INPs to induce order in the hydration layer and …

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 …

The ice/water interface recognition mechanism of antifreeze proteins (AFPs) is highly
contentious. Conventionally, protein adsorption on a solid surface is primarily driven by the …

Clathrate hydrate forms when a hydrophobic molecule is entrapped inside a water cage or
cavity. Although biomolecular structures also have hydrophobic patches, clathrate-like water …

Antifreeze proteins (AFPs) have unique features to sustain life in sub-zero environments due
to ice recrystallization inhibition (IRI) and thermal hysteresis (TH). AFPs are in demand as …

Study of cold denaturation is relevant for understanding the freeze tolerant activity of
organism at sub-zero environment. The proteins responsible for the survival of these …

Like hyperactive antifreeze proteins (AFPs), globular AFPs also illustrate thermal hysteresis
by specific binding to ice. The ice‐binding surface (IBS) topology and residue preferences …

Organisms living in extreme cold conditions find a unique solution for cold adaptation. They
produce a group of proteins, called antifreeze proteins (AFPs) which cause depression of …