Determination of the chain-folding pattern in the crystalline domains of the repetitive polypeptide {(AlaGly)_3GluGly(GlyAla)_3GluGly}_10 by FTIR studies of its blends with a ^(13)C-enriched analog

We are interested in the design and characterization of repetitive polypeptides that assemble into lamellae of uniform, predetermined thickness (Figure 1). In the initial stages of this work, the design of the polypeptide repeating unit (which comprises a sequence of amino acids traversing the thickness of the lamella and a turn sequence) has been based in part on work on the structure of silk and its analogues and in part on the literature on reverse turns in globular protein. In particular, we have reported the synthesis and characterization of polypeptides comprising repeating unit sequences 1-3.