Cytochrome c(551) as a model system for protein folding
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Updated: Sep 26, 2026

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
Published on: December 18, 2013
Maurizio Brunori1, Maria Giulia Bigotti, Francesca Cutruzzolà
1Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Università di Roma La Sapienza, P. le A. Moro 5, 00185 Roma, Italy. maurizio.brunori@uniroma1.it
Abstract:
Considerable progress was made over the last few years in understanding the mechanism of folding of cytochrome c(551), a small acidic hemeprotein from Pseudomonas aeruginosa. Comparison of our results with those obtained by others on horse heart cytochrome c allows to draw some general conclusions on the structural features that are common determinants in the folding of members of the cytochrome c family.
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