Related papers: Kinetic pinning and biological antifreezes
The fascinating ability of algae, insects and fishes to survive at temperatures below normal freezing is realized by antifreeze proteins (AFPs). These are surface-active molecules and interact with the diffusive water/ice interface thus…
Antifreeze proteins (AFPs) evolved in cold-adapted organisms and serve to protect them against freezing in cold conditions by arresting ice crystal growth. Recently, we have shown quantitatively that adsorption of AFPs not only prevents ice…
Antifreeze proteins (AFPs) are remarkable biomolecules that suppress ice formation at trace concentrations. To inhibit ice growth, AFPs must not only bind to ice crystals, but also resist engulfment by ice. The highest supercooling, $\Delta…
Antifreeze proteins (AFPs) are the sub-set of ice binding proteins indispensable for the species living in extreme cold weather. These proteins bind to the ice crystals, hindering their growth into large ice lattice that could cause…
In extreme cold weather, living organisms produce Antifreeze Proteins (AFPs) to counter the otherwise lethal intracellular formation of ice. Structures and sequences of various AFPs exhibit a high degree of heterogeneity, consequently the…
A basically new Hierarchic theory, general for solids and liquids (Kaivarainen, 2001, 2000, 1995, 1992), has been briefly described and illustrated by computer simulations on examples of water and ice. Full description of theory and its…
The melting of pure axisymmetric ice crystals has been described previously by us within the framework of so-called geometric crystal growth. Nonequilibrium ice crystal shapes evolving in the presence of hyperactive antifreeze proteins…
Crystal faceting can emerge via two broad physical mechanisms: anisotropic attachment kinetics on growing crystals and anisotropic surface energies on near-equilibrium crystals. For the case of the ice/vapor system, anisotropic attachment…
We present a statistical mechanics treatment of the stability of globular proteins which takes explicitly into account the coupling between the protein and water degrees of freedom. This allows us to describe both the cold and the warm…
As an example of topic where biology and physics meet, we present the issue of protein folding and stability, and the development of thermodynamics-based bioinformatics tools that predict the stability and thermal resistance of proteins and…
The atomic displacements associated with the freezing of metals and salts are calculated by treating crystal growth as an assignment problem through the use of an optimal transport algorithm. Converting these displacements into time scales…
Hypothesis Roughening transitions at solid-liquid interfaces govern crystal morphology in diverse systems. In ice crystallization, these transitions control interfacial faceting and surface kinetics. Faceted morphologies are often…
Heterogeneous ice growth exhibits a maximum in freezing rate arising from the competition between kinetics and the thermodynamic driving force between the solid and liquid states. Here, we use molecular dynamics simulations to elucidate the…
Proteins fold to a specific functional conformation with a densely packed hydrophobic core that controls their stability. We develop a geometric, yet all-atom model for proteins that explains the universal core packing fraction of…
Neither of the two prevalent theories, namely thermodynamic stability and kinetic stability, provides a comprehensive understanding of protein folding. The thermodynamic theory is misleading because it assumes that free energy is the…
For the contact of two finite portions of interacting rigid crystalline surfaces, we compute the dependence of the pinning energy barrier on the misfit angle and contact area. The resulting data are used to investigate the distribution of…
Knotted proteins embed a physical (i.e., open) knot within their native structures. For decades, significant effort has been devoted to elucidating the functional role of knots in proteins, yet no consensus has been reached. Here, using…
Folding kinetics of a lattice model of protein is studied. It uses the Random Energy Model for the intrachain couplings and a temperature dependent free energy of solvation derived from a realistic hydration model of apolar solutes. The…
Arginine has been a mainstay in biological formulation development for decades. To date, the way arginine modulates protein stability has been widely studied and debated. Here, we employed a hydrophobic polymer to decouple hydrophobic…
Antifreeze glycoproteins (AFGPs) are among the most potent ice recrystallization inhibition (IRI) agents, yet the molecular basis for their counterintuitive decline in activity with increasing glycosylated threonine (T*) content remains…