  Proteins appear to be the most dramatic natural example of self-organized
criticality (SOC), a concept that explains many otherwise apparently unlikely
phenomena. Protein functionality is dominated by long range
hydro(phobic/philic) interactions which both drive protein compaction and
mediate protein-protein interactions. In contrast to previous reductionist
short range hydrophobicity scales, the holistic Moret-Zebende hydrophobicity
scale represents a hydroanalytic tool that bioinformatically quantifies SOC in
a way fully compatible with evolution. Hydroprofiling identifies chemical
trends in the activities and substrate binding abilities of model enzymes and
antibiotic animal lysozymes c and antibiotic human defensins, which have been
the subject of tens of thousands of experimental studies. The analysis is
simple and easily performed, and immediately yields insights not obtainable by
traditional methods based on short-range real-space interactions, as described
either by classical force fields (CFF) used in molecular dynamics simulations
(MDS), or hydrophobicity scales based on transference energies from water to
organic solvents.
