Reversible redox reconfiguration of secondary structures in a designed peptide

Xiaojian Wang, Irina Bergenfeld, Paramjit S. Arora, James W. Canary

Research output: Contribution to journalArticle

Abstract

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/CuII.

Original languageEnglish (US)
Pages (from-to)12099-12101
Number of pages3
JournalAngewandte Chemie - International Edition
Volume51
Issue number48
DOIs
StatePublished - Nov 26 2012

Keywords

  • peptide switches
  • peptides
  • protein structures
  • redox chemistry

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Fingerprint Dive into the research topics of 'Reversible redox reconfiguration of secondary structures in a designed peptide'. Together they form a unique fingerprint.

  • Cite this