Reversible redox reconfiguration of secondary structures in a designed peptide

Xiaojian Wang, Irina Bergenfeld, Paramjit Arora, James 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

Fingerprint

Peptides
Protein folding
Conformations
Monomers
Proteins
Oxidation
Electrons
Oxidation-Reduction

Keywords

  • peptide switches
  • peptides
  • protein structures
  • redox chemistry

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

Reversible redox reconfiguration of secondary structures in a designed peptide. / Wang, Xiaojian; Bergenfeld, Irina; Arora, Paramjit; Canary, James.

In: Angewandte Chemie - International Edition, Vol. 51, No. 48, 26.11.2012, p. 12099-12101.

Research output: Contribution to journalArticle

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