Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY
Volume 173, Issue 1, Pages 21-28Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotochem.2004.12.026
Keywords
azobenzene; alpha-helix-coil; light-induced; photo-control; photo-isomerization
Categories
Ask authors/readers for more resources
Reversible photo-control of protein structure and function is used by Nature to direct complex biological response to light. Reversibility is a feature that has been difficult to reliably achieve in analogous biomimetic systems. We report here measurement of the thermal and photoisomerization rates for peptide model systems in which isomerization of an intramolecularly linked azobenzene unit causes a helix-coil transition in the peptide. Reversibility is maintained and indeed the quantum yield for cis-to-trans photoisomerization is enhanced in these systems compared to an unstructured glutathione adduct of the chromophore alone. Reversibility can be understood by considering the intrinsic conformational preferences of the peptides to which the linkers are attached and how these preferences impact the stabilities of the transition states for isomerization. (c) 2004 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available