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Large Circular Dichroism Ellipticities for N‐Templated Helical Polypeptides Are Inconsistent with Currently Accepted Helicity Algorithms
Author(s) -
Wallimann Peter,
Kennedy Robert J.,
Kemp Daniel S.
Publication year - 1999
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/(sici)1521-3773(19990503)38:9<1290::aid-anie1290>3.0.co;2-e
Subject(s) - helicity , circular dichroism , helix (gastropod) , peptide , crystallography , stereochemistry , chemistry , physics , biology , biochemistry , particle physics , ecology , snail
An unprecedented , high degree of helicity as judged by CD spectroscopy is observed in N‐templated model peptides of the type AcHel‐(Ala 4 Lys) n Ala 2 ‐NH 2 (AcHel‐Ala peptide pictured; AcHel is an N‐terminal helix‐inducing template for polypeptides). These results raise concern over the current methods for determining 100 % helicity.