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Conserved nucleation sites reinforce the significance of phi analysis in proteinfolding studies
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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
Abstract [en]

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.
Keyword [en]
Protein Folding, kinetics, mutagenesis, homologous proteins
National Category
Medical and Health Sciences Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-228447DOI: 10.1002/iub.1287ISI: 000340575200001PubMedID: 25044918OAI: oai:DiVA.org:uu-228447DiVA: diva2:734146
Available from: 2014-07-15 Created: 2014-07-15 Last updated: 2017-12-05Bibliographically approved

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Jemth, Per

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