Determination of homopolypeptide conformational changes by the modeling of electrophoretic mobilities

This work deals with the modeling of electrophoretic mobilities of end-charged homopolypeptides. The ionic mobilities of six families of homopolypeptides (polyglycines, poly-L-alanines, poly-L-valines, poly-L-leucines, poly-L-isoleucines, and poly-L-phenylalanines), with polymerization degrees up to 11, have been carefully determined. The electrophoretic frictional coefficients derived from the ionic mobility values were modeled by the hydrodynamic frictional coefficient of an equivalent cylinder. The hydrodynamic modeling allowed the determination of the molecular dimensions of the homopolypeptides in the electrolyte. The results were in good accordance with the expected geometry of the molecules. This approach allows monitoring the change in peptide conformations as a function of the experimental conditions (temperature, nature of the solvent) through the determination of geometrical molecular parameters (total peptide length, lateral radius of the equivalent cylinder, and folding angle). The influence of the bulkiness of the homopolypeptide lateral chain on the conformation is also discussed.