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Reversible Redox Reconfiguration of Secondary Structures in a Designed Peptide
Author(s) -
Wang Xiaojian,
Bergenfeld Irina,
Arora Paramjit S.,
Canary James W.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201206009
Subject(s) - peptide , redox , folding (dsp implementation) , control reconfiguration , monomer , chemistry , protein folding , protein secondary structure , aggregate (composite) , function (biology) , biophysics , crystallography , nanotechnology , materials science , computer science , biochemistry , inorganic chemistry , biology , organic chemistry , microbiology and biotechnology , engineering , polymer , electrical engineering , embedded system
Secondary structures are critical regulators of protein structure and function. Switchable peptides that can adopt multiple defined conformations in response to stimuli are attractive model systems for the study of protein folding and misfolding. A peptide is presented that can be reversibly reconfigured between an α‐helical monomer and a β‐sheet aggregate upon one‐electron oxidation and reduction in the presence of Cu I /Cu II .