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 D. Hamilton

doi:10.1021/ja028574m

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 D. Hamilton

Chemistry

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	4420-4421
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	15
DOIs	https://doi.org/10.1021/ja028574m
State	Published - Apr 16 2003

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja028574m

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title = "Directed denaturation: Room temperature and stoichiometric unfolding of cytochrome c by a metalloporphyrin dimer",

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.",

author = "Wilson, {Andrew J.} and Kevin Groves and Jain, {Rishi K.} and Park, {Hyung Soon} and Hamilton, {Andrew D.}",

year = "2003",

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doi = "10.1021/ja028574m",

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T2 - Room temperature and stoichiometric unfolding of cytochrome c by a metalloporphyrin dimer

AU - Wilson, Andrew J.

AU - Groves, Kevin

AU - Jain, Rishi K.

AU - Park, Hyung Soon

AU - Hamilton, Andrew D.

PY - 2003/4/16

Y1 - 2003/4/16

N2 - 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.

AB - 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.

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JO - Journal of the American Chemical Society

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IS - 15

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

Abstract

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