Conserved nucleation sites reinforce the significance of phi analysis in proteinfolding studies
2014 (English)In: IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, ISSN 1521-6543, E-ISSN 1521-6551, Vol. 66, no 7, 449-452 p.Article in journal (Refereed) Published
The only experimental strategy to address the structure of folding transition states, theso-called Φ value analysis, relies on the synergy between site directed mutagenesisand the measurement of reaction kinetics. Despite its importance, the Φ value analysishas been often criticized and its power to pinpoint structural information has beenquestioned. In this Hypothesis we demonstrate that comparing the Φ values betweenproteins not only allows highlighting the robustness of folding pathways, but alsoprovides per se a strong validation of the method.
Place, publisher, year, edition, pages
2014. Vol. 66, no 7, 449-452 p.
Protein Folding, kinetics, mutagenesis, homologous proteins
Medical and Health Sciences Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-228447DOI: 10.1002/iub.1287ISI: 000340575200001PubMedID: 25044918OAI: oai:DiVA.org:uu-228447DiVA: diva2:734146