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.
authors.affiliation: Department of Chemistry, P.O. Box 208107, 225 Prospect Street, Yale University, New Haven, CT 06520-8107, USA.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Wilson
authors.forename: Kevin
authors.initials: K
authors.lastname: Groves
authors.forename: Rishi K
authors.initials: RK
authors.lastname: Jain
authors.forename: Hyung Soon
authors.initials: HS
authors.lastname: Park
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Hamilton
mesh_terms: 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
chemical_list: D003574:Cytochrome c Group; D008665:Metalloporphyrins; D003300:Copper; D015032:Zinc