A simple atomic-level hydrophobicity scale reveals protein interfacial structure.

Many amino acid residue hydrophobicity scales have been created in an effort to better understand and rapidly characterize water-protein interactions based only on protein structure and sequence. There is surprisingly low consistency in the ranking of residue hydrophobicity between scales, and their ability to provide insightful characterization varies substantially across subject proteins. All current scales characterize hydrophobicity based on entire amino acid residue units.

Entropy production in chiral symmetry breaking transitions.

It is now well known that nonequilibrium chemical systems may reach conditions that spontaneously generate chiral asymmetry. One can find a host of model reactions that exhibit such behavior in the literature. Among these, models based on one originally devised by Frank have been studied extensively.