From Atomic Nuclei to Drug Design

The concepts developed to quantitatively describe the variety of phase transitions displayed by atomic nuclei as a function of mass number, isospin, rotational frequency and temperature (spherical-deformed, normal-superfluid, etc.) taken properly into account fluctuations and quantal size effect are shown to provide not only a powerful framework to describe the phase transition displayed by proteins between the denaturated state and the native, biologically active conformation, but also the basis for a bona fide model solution of the protein folding problem and the design of non-conventional drugs which do not suffer from drug resistance generated by mutations. The extension of these results to real proteins depends on the ability to calculate the interaction between few, strongly interacting (as a rule hydrophobic) amino acids from first priciples, an ability we have developed through the years in mapping out the interdisciplinarity field of research dealing with finite quantal many-body systems like atomic nuclei, metal clusters and fullerenes, lying at the borderline between nuclear and solid state physics.