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Parallel Sheet Secondary Structure in β‐Peptides
Author(s) -
Langenhan Joseph M.,
Guzei Ilia A.,
Gellman Samuel H.
Publication year - 2003
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/anie.200350932
Subject(s) - linker , beta sheet , folding (dsp implementation) , protein secondary structure , chemistry , peptide , diamine , amino acid , crystallography , stereochemistry , polymer chemistry , biochemistry , computer science , electrical engineering , engineering , operating system
Diamine‐linked syn ‐α,β‐dialkyl β‐amino acid residues (see picture) have been shown to exhibit parallel sheet secondary structure. Adoption of the parallel hairpin folding pattern is less strongly influenced by linker stereochemistry than for similar parallel hairpins in analogous α‐peptide systems.