World Scientific Review Volume -9.75in x 6.5in 120507˙˙more˙is˙diff 2 R.A. Broglia acids occurring in nature, and the associated symmetry breaking in information (sequence) space. Emergent properties of the corresponding phase transition are domain walls which stabilize local elementary structures (LES), few groups of 10-20 aminoacids which become structured already in the denatured state with varied degree of stability, and which can be viewed as (mutually complementary) virtual secondary structures providing the molecular recognition directing protein folding under biological conditions (solvent, temperature, pH, etc.). In fact, their docking is closely related to the transition state of the process. While the two-step, yes or no, folding process, does not provide direct information concerning LES, one can force LES from virtual to become real, observable final state entities. Getting again inspiration from the nuclear case (virtual processes contributing to pair correlations can be forced to become real with the help of a probe which itself changes particle number by two), one would expect that to make real virtual LES, that is segments of the protein which already at an early stage of the folding process flicker in and out of their native conformation, one needs a probe which itself displays a similar behaviour. It is almost self-evident that peptides (p-LESi) displaying a sequence identical to LESi will bind with high specificity to its complementary LESj, blocking folding and exposing the (p-LES)i-LESj complex to direct observation. Results in vitro and ex vivo (infected cells) of the folding inhibition ability of p-LES, testify to the soundness of the picture. Based again on the analogy with the nuclear case (become theoretically and experimentally quantitative in the prediction and measurements of Cooper-pair tunneling), much effort has been concentrated in defining the new paradigm of protein inhibition, namely folding inhibition, and to develop the in silica protocols, and the wet laboratory activity assays, which quantitatively can map out the role LES play in folding. It is expected that eventually, this insight can help in developing p-LES into leads of non-conventional drugs.