796881-89-5Relevant academic research and scientific papers
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 D.
, p. 4420 - 4421 (2003)
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. Copyrigh
Catalytic unfolding and proteolysis of cytochrome c induced by synthetic binding agents
Groves, Kevin,Wilson, Andrew J.,Hamilton, Andrew D.
, p. 12833 - 12842 (2007/10/03)
A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibility of cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. The free energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol in the bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalent of metalloporphyrin to effect complete, rapid digestion in the presence of a protease.
