PNNL

Abstract

The a-helix – the common building block of the protein secondary structure - plays an important role in determining protein structure and function. The biological function of the a-helix is mainly attributed to its large macrodipole originating from the alignment of individual dipole moments of peptide bonds. Preparation of directionally aligned a-helical peptide layers on substrates has attracted significant attention because the resulting strong net dipole is useful for a variety of applications in photonics, , molecular electronics, and catalysis. - In addition, conformationally-selected a-helical peptide arrays can be used for detailed characterization of molecular recognition steps critical for protein folding, enzyme function and DNA binding by proteins. Existing technologies for the production of a-helical peptide surfaces are based on a variety of solution phase synthetic strategies - that usually require relatively large quantities of purified materials.