Premium
cis ‐2‐Aminocyclopentanecarboxylic Acid Oligomers Adopt a Sheetlike Structure: Switch from Helix to Nonpolar Strand
Author(s) -
Martinek Tamás A.,
Tóth Gábor K.,
Vass Elemér,
Hollósi Miklós,
Fülöp Ferenc
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20020517)41:10<1718::aid-anie1718>3.0.co;2-2
Subject(s) - helix (gastropod) , chemistry , rational design , stereochemistry , amino acid residue , crystallography , computer science , peptide sequence , biochemistry , materials science , biology , nanotechnology , gene , ecology , snail
Rational control over helix and strand secondary structures is possible when conformationally restricted cyclic β ‐amino acid residues are incorporated in the β ‐peptides. Inversion of the relative configuration of these residues enables the preferred periodic structure to be switched from a helix to a single nonpolar strand (see picture).