Cover Picture: Solvent Polarity Controls the Helical Conformation of Short Peptides Rich in Cα-Tetrasubstituted Amino Acids (Chem. Eur. J. 2/2007)

Like shock absorbers in cars short helical peptides rich in C α ‐tetrasubstituted amino acids change their elongation responding to an external stimulus. In fact, they behave like molecular springs and adjust their conformation according to the polarity of the medium in which they are dissolved. In...

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Bibliographic Details
Published in:Chemistry : a European journal 2007-01, Vol.13 (2), p.367-367
Main Authors: Bellanda, Massimo, Mammi, Stefano, Geremia, Silvano, Demitri, Nicola, Randaccio, Lucio, Broxterman, Quirinus B., Kaptein, Bernard, Pengo, Paolo, Pasquato, Lucia, Scrimin, Paolo
Format: Article
Language:English
Subjects:
helical structures
NMR spectroscopy
peptides
solvent effects
structure elucidation
Online Access:Get full text
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Summary:Like shock absorbers in cars short helical peptides rich in C α ‐tetrasubstituted amino acids change their elongation responding to an external stimulus. In fact, they behave like molecular springs and adjust their conformation according to the polarity of the medium in which they are dissolved. In solvents of high polarity (like water) they shrink, adopting an α‐helix conformation, while in solvents of low polarity (like isopropanol) they elongate, adopting a 3 10 ‐helix conformation. Details of this behavior are to be found in the Full Paper by P. Scrimin, S. Mammi, L. Randaccio, L. Pasquato et al. on page 407 ff.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.200790003