Article
Protein stability and mutations in the axial methionine loop of a minimal cytochrome c.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Jul 2004
Bartalesi Ilaria, Bertini Ivano, Di Rocco Giulia, Ranieri Antonio, Rosato Antonio, Vanarotti Murugendra, Vasos Paul R, Viezzoli Maria Silvia
Abstract excerpt
The minimal mono-heme ferricytochrome c from Bacillus pasteurii, containing 71 amino acids, has been further investigated through mutagenesis of different positions in the loop containing the iron ligand Met71. These mutations have been designed to sample different aspects of the loop structure, in order to obtain insights into the determinants of the stability of the iron(III) environment. In particular,...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.