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Cover Picture: Solvent Polarity Controls the Helical Conformation of Short Peptides Rich in C α ‐Tetrasubstituted Amino Acids (Chem. Eur. J. 2/2007)
Author(s) -
Bellanda Massimo,
Mammi Stefano,
Geremia Silvano,
Demitri Nicola,
Randaccio Lucio,
Broxterman Quirinus B.,
Kaptein Bernard,
Pengo Paolo,
Pasquato Lucia,
Scrimin Paolo
Publication year - 2007
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200790003
Subject(s) - polarity (international relations) , solvent polarity , chemistry , solvent , elongation , amino acid , helix (gastropod) , crystallography , stereochemistry , peptide , biophysics , materials science , biochemistry , biology , snail , cell , metallurgy , ultimate tensile strength , ecology
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.