Issue 77, 2012

Allosteric effects in coiled-coil proteins folding and lanthanide-ion binding

Abstract

Peptide sequences modified with lanthanide-chelating groups at their N-termini, or at their lysine side chains, were synthesized, and new Ln(III) complexes were characterized. We show that partial folding of the conjugates to form trimer coiled coil structures induces coordination of lanthanides to the ligand, which in turn further stabilizes the 3D structure.

Graphical abstract: Allosteric effects in coiled-coil proteins folding and lanthanide-ion binding

Supplementary files

Article information

Article type
Communication
Submitted
18 Jul 2012
Accepted
05 Aug 2012
First published
06 Aug 2012

Chem. Commun., 2012,48, 9577-9579

Allosteric effects in coiled-coil proteins folding and lanthanide-ion binding

M. Samiappan, S. Alasibi, R. Cohen-Luria, A. Shanzer and G. Ashkenasy, Chem. Commun., 2012, 48, 9577 DOI: 10.1039/C2CC35166H

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