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Double helix formation in α‐peptides: a theoretical study
Author(s) -
Schramm Peter,
Hofmann HansJörg
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1234
Subject(s) - antiparallel (mathematics) , chemistry , peptide , helix (gastropod) , hydrogen bond , crystallography , ab initio , stereochemistry , collagen helix , rational design , molecular dynamics , triple helix , computational chemistry , molecule , materials science , physics , nanotechnology , biochemistry , biology , organic chemistry , quantum mechanics , snail , magnetic field , ecology
A complete overview on all possible hydrogen bonding patterns of double helices with antiparallel and parallel strand orientation in α‐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. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.