Recent contributions of electronic circular dichroism to the investigation of oligopeptide conformations

Recent applications in our laboratories of electronic circular dichroism to the study of peptide secondary structures and their changes under external stimuli are briefly reviewed. More specifically, this article deals with: 1) characterization of a novel peptide conformation; 2) origin of amino aci...

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Bibliographic Details
Published in:Chirality (New York, N.Y.) N.Y.), 2004, Vol.16 (6), p.388-397
Main Authors: Formaggio, Fernando, Peggion, Cristina, Crisma, Marco, Kaptein, Bernard, Broxterman, Quirinus B., Mazaleyrat, Jean-Paul, Wakselman, Michel, Toniolo, Claudio
Format: Article
Language:English
Subjects:
310-helix
Chemistry - methods
circular dichroism
Circular Dichroism - methods
Models, Chemical
Molecular Conformation
Oligopeptides - chemistry
peptides
Peptides - chemistry
Protein Conformation
Protein Structure, Secondary
Time Factors
transfer of chirality
α-helix
β-turn
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Summary:Recent applications in our laboratories of electronic circular dichroism to the study of peptide secondary structures and their changes under external stimuli are briefly reviewed. More specifically, this article deals with: 1) characterization of a novel peptide conformation; 2) origin of amino acid homo‐chirality on Earth; 3) bend and helical peptides as spacers; and 4) transfer and propagation of chirality in peptides. Chirality 16:388–397, 2004. © 2004 Wiley‐Liss, Inc.
ISSN:0899-0042
1520-636X
DOI:10.1002/chir.20051