Abstract
A complete overview on all possible hydrogen bonding patterns of double helices with antiparallel and parallel strand orientation in alpha-peptide sequences is provided on the basis of ab initio molecular orbital theory. The most stable representatives belong to the group of antiparallel helices. The study on side chain influence shows that these double helices can only be realized if the strands are composed of L- and D-amino acids in alternate order. The stability of the double helices is compared with that of competing single-stranded helices. The data contribute to an understanding of secondary structure formation in peptides and provide a basis for a rational design of membrane channels.
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