Directed Denaturation: Room Temperature and Stoichiometric Unfolding of Cytochrome c by a Metalloporphyrin Dimer
摘要:
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.
Protein Surface Recognition by Synthetic Receptors Based on a Tetraphenylporphyrin Scaffold
作者:Rishi K. Jain、Andrew D. Hamilton
DOI:10.1021/ol005871s
日期:2000.6.1
[GRAPHICS]Receptors based on a tetraphenylporphyrin scaffold bearing different charged and hydrophobic groups have been synthesized, The interactions of these with horse heart cytochrome c were studied by fluorescence spectroscopy. Receptor 4 was identified to be the strongest synthetic receptor (K-d = 20 nM) for cytochrome c. The differences in affinity among the receptors reflected a dependence on the number of anionic and hydrophobic groups.