Professinal Experinence: Professor Ali A. Moosavi-Movahedi's scientific career has been mostly marked on thermodynamics of protein denaturation especially by surfactants, protein folding/unfolding, protein glycation, artificial enzyme and bioactive peptides. Denaturation study provides extra information on local and site-specific properties of biological macromolecule systems that lie at the heart of many biochemical regulation phenomena and are the basic key to biological control. Protein denaturation is a key technique to obtain the stability of protein in solution and understanding the protein function-structure relationship. The denaturation by surfactants provide the specific virtue of directly binding between biological macromolecules (e.g. protein, DNA) and surfactant complexes. The availability of binding data induced the chance to open up the way to extensive area of macromolecular ligand binding theories that provide a deep understanding of macromolecular interactions and cooperativity. He has also theorized and coins the terminology of "hydrophobic salts" in the literature for surfactants at low concentrations upon interaction with proteins. He is also extensively involved on biophysics of molecular diabetes on the area of protein glycation and studies the amyloid and fibril products in cellular and molecular actions. He has been elected to the UNESCO Chair on Interdisciplinary Research in Diabetes, at University of Tehran(ucird.ut.ac.ir), whereby he will lead a research study in molecular diabetes and define the theme "oxidative stress stimulates diabetes".