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Probing the conformation of a polypeptide on a Si(111)-(4x1) surface by H/D isotopic exchange and single scattering events.
The relation between the formation of the secondary structure of alpha-chymotrypsin, its adsorption and the single scattering events occurring on its surface was studied by means of vibrational spectroscopy, (H/D) isotopic exchange and SAXS analysis. The first two methods combined were found to be effective tools to probe alpha-chymotrypsin and other proteins adsorbed on metallic substrates. The results show that alpha-chymotrypsin adopts a two-fold symmetric conformation on the surface with a predominant alpha-helical content, and it also clearly suggests that a part of the trypsin-like enzymatic activity of alpha-chymotrypsin is still preserved when bound to 0b46394aab