Directed denaturation: room temperature and stoichiometric unfolding of cytochrome C by a metalloporphyrin dimer.
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.
Wilson
Andrew J
AJ
Department of Chemistry, P.O. Box 208107, 225 Prospect Street, Yale University, New Haven, CT 06520-8107, USA.
Groves
Kevin
K
Jain
Rishi K
RK
Park
Hyung Soon
HS
Hamilton
Andrew D
AD
D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008665:Metalloporphyrins / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D015032:Zinc / Q000737:chemistry
D003574:Cytochrome c Group; D008665:Metalloporphyrins; D003300:Copper; D015032:Zinc