American Chemical Society, Journal of the American Chemical Society, 6(129), p. 1532-1533, 2007
DOI: 10.1021/ja068678n
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We recently reported that beta-peptides can form discrete hetero-oligomers in aqueous solution. Here we describe the structure of such an oligomer as determined by X-ray crystallography. The structure of Zwit-1F reveals a homo-octamer of two cupped "hands" composed of both parallel and antiparallel 3(14)-helices. The core of the assembly is composed entirely of solvent-excluded beta(3)-homoleucine residues. The Zwit-1F assembly shares many of the physical characteristics of natural proteins.