Conserved nucleation sites reinforce the significance of Phi value analysis in protein-folding studies.

Stefano Gianni (1, 2) , Per Jemth (3)

1 Department of Chemistry [Cambridge, UK]
2 Department of Biochemical Sciences "Rossi Fanelli"
3 Department of Medical Biochemistry and Microbiology

The only experimental strategy to address the structure of folding transition states, the so-called Φ value analysis, relies on the synergy between site directed mutagenesis and the measurement of reaction kinetics. Despite its importance, the Φ value analysis has been often criticized and its power to pinpoint structural information has been questioned. In this hypothesis, we demonstrate that comparing the Φ values between proteins not only allows highlighting the robustness of folding pathways but also provides per se a strong validation of the method.

Mots clés: protein folding; kinetics; mutagenesis; homologous proteins

Domaines: Biochimie, Biologie Moléculaire

Stefano Gianni, Per Jemth. Conserved nucleation sites reinforce the significance of Phi value analysis in protein-folding studies.. IUBMB Life, 2014, 66 (7), pp.449-52. ⟨10.1002/iub.1287⟩. ⟨pasteur-01181367⟩