Hydroanalysis of Animal Lysozymes c and Human Defensins a

TL;DR

This paper introduces a holistic hydroanalytic scale to analyze protein interactions, revealing chemical trends in enzymes and defensins that traditional methods overlook, emphasizing the role of self-organized criticality in protein function.

Contribution

It presents a new bioinformatics hydroanalytic tool based on the Moret-Zebende scale, offering insights into protein activity and substrate binding beyond traditional short-range interaction methods.

Findings

Hydroprofiling reveals chemical trends in enzyme activities.

The method uncovers insights not accessible by classical force fields.

Analysis is simple and compatible with evolutionary data.

Abstract

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.