Cross-talk between structures: proteins, water and the environment

PERILLO MA

Santiago del Estero

Congreso; XLIV Reunión Anual de la Sociedad Argentina de Biofísica (SAB); 2015

Sociedad Argentina de Biofísica

Classical biochemistry has dealt with thereactions that occur in perfectly homogeneus media and fully dilutedconditions. By contrast, most real systems, such as the cytoplasm, areheterogeneous and macromolecularly crowded environments. There, thethermodynamic activity of solvent and those of the solutes are far from idealconditions. These heterogeneous environments offer numerous interfaces anddynamic compartments. The confinement of the reactions in a dimensionallyconstrained space such as a percolation matrix or a surface, may causesignificant effects on the mechanism and rate of reactions. In these crowdedenvironments, water exhibits a restricted availability as a solvent. Hence, ofthe hydrophobic effect, the driving force for protein folding and self-assemblyof biomembrane components, are also affected. Framed within these concepts,results on the modulation of protein activity exerted by the dynamicorganization changes in its molecular environment will be presented. Thisactivity involves the binding of a ligand (or substrate) and the transductionof binding into function. We will discuss about the dimensionality of themedium and the water structure affecting these phenomena.