Large Circular Dichroism Ellipticities for N-Templated Helical Polypeptides Are Inconsistent with Currently Accepted Helicity Algorithms

An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N‐templated model peptides of the type AcHel‐(Ala4Lys)nAla2‐NH2 (AcHel‐Ala peptide pictured; AcHel is an N‐terminal helix‐inducing template for polypeptides). These results raise concern over the current methods fo...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 1999-05, Vol.38 (9), p.1290-1292
Main Authors: Wallimann, Peter, Kennedy, Robert J., Kemp, Daniel S.
Format: Article
Language:English
Subjects:
Circular dichroism
Helical structures
Peptides
Online Access:Get full text
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Summary:An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N‐templated model peptides of the type AcHel‐(Ala4Lys)nAla2‐NH2 (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.
ISSN:1433-7851
1521-3773
DOI:10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E