Abstract
We have investigated the intermediate structures in the self-assembly of a peptide (of sequence FKFEFKFE) designed with alternating polar and nonpolar amino acids. Self-assembly was followed over time using atomic force microscopy, transmission electron microscopy and circular dichroism. Molecular dynamics simulations suggest that these intermediates are left-handed double helical /spl beta/-sheets. These findings have implications in the study of protein conformational diseases and in the molecular design of materials.
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