Directed denaturation: Room temperature and stoichiometric unfolding of cytochrome c by a metalloporphyrin dimer

Andrew J. Wilson, Kevin Groves, Rishi K. Jain, Hyung Soon Park, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

Using circular dichroism, UV-vis, and trypsin proteolysis, we have shown how a metalloporphyrin dimer induces the unfolding of a protein, cytochrome c, under physiologically relevant conditions and accelerates its rate of proteolytic degradation.

Original languageEnglish (US)
Pages (from-to)4420-4421
Number of pages2
JournalJournal of the American Chemical Society
Volume125
Issue number15
DOIs
StatePublished - Apr 16 2003

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Metalloporphyrins
Proteolysis
Protein Unfolding
Denaturation
Circular Dichroism
Cytochromes c
Dimers
Trypsin
Proteins
Degradation
Temperature
Dichroism

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Directed denaturation : Room temperature and stoichiometric unfolding of cytochrome c by a metalloporphyrin dimer. / Wilson, Andrew J.; Groves, Kevin; Jain, Rishi K.; Park, Hyung Soon; Hamilton, Andrew.

In: Journal of the American Chemical Society, Vol. 125, No. 15, 16.04.2003, p. 4420-4421.

Research output: Contribution to journalArticle

Wilson, Andrew J. ; Groves, Kevin ; Jain, Rishi K. ; Park, Hyung Soon ; Hamilton, Andrew. / Directed denaturation : Room temperature and stoichiometric unfolding of cytochrome c by a metalloporphyrin dimer. In: Journal of the American Chemical Society. 2003 ; Vol. 125, No. 15. pp. 4420-4421.
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