Senior Investigator, Argentine National Research Council
Ariel Fernandez is a Senior Investigator of Argentine National Research Council. Ariel Fernández introduced what appears to be the correct formulation for self-organization in nonequilibrium thermodynamics by realizing that the thermodynamically relevant degrees of freedom must belong to a center manifold, an algebraically closed entity, and not to an attractor, as Ilya Prigogine previously assumed. He has provided a semiempirical solution to the protein folding problem by introducing the episteric tension, a measure of the distortion of the water structural matrix that requires a multi-scale theory of dielectrics. He rationally discovered a ligand that would competitively disrupt a protein-protein interface for therapeutic purposes.
He also managed to predict and control induced folding in drug-target associations. He introduced the dehydron, a structural defect in proteins that promotes its own dehydration. A dehydron is a meta-structural feature of relevance in drug design, enzyme catalysis and protein folding. Ariel Fernández determined and measured the dehydronic field, the mechanical equivalent of the dehydration propensity of a dehydron exerted on a test nonpolar molecule and orthogonal to the Coulombic field. His current efforts are devoted to show that dehydrons are enablers and stimulators of enzyme catalysis.
Pharmacoinformatics and Pharmacogenomics; Translational Medical Informatics; Molecularly Targeted Cancer Therapy; Clinical Kinomics; Integrative Biology; Bioinformatics; Discovery Informatics; Systems Bioengineering; Molecular Theranostic Engineering; Physical Chemistry; Molecular Biophysics, Dehydron Physics