Abstract
The molecular chaperone DnaK was optimized by directed evolution for better refolding activity toward two substrates and the identified DnaK variants were analyzed for characteristic changes in their mechanism. Remarkably, none of the variants was modified in or in close proximity to the substrate binding pocket, although their substrate affinity was increased. These results indicate that improvement in chaperone activity for specific substrates does not necessarily decrease substrate promiscuity.
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Regina Simone Schweizer 2001–2007 Studium der Chemie an der Universität Stuttgart mit Diplomarbeit im Fachbereich Biochemie bei Prof. D. H. Wolf, 2008–2011 Promotion am MPI für medizinische Forschung in Heidelberg in der Arbeitsgruppe von PD Dr. J. Reinstein, Abteilung Biomolekulare Mechanismen.
Jochen Reinstein 1981–1987 Biologiestudium an der Universität Heidelberg, 1987–1990 Promotion bei Prof. Dr. F. Wittinghofer. 1990–1992 Postdoc an der Brandeis University, Waltham, MA, USA, bei Prof. Dr. B. Jencks, 1993–2003 Gruppenleiter am Max-Planck-Institut für molekulare Physiologie, Dortmund. 2000 Habilitation für das Fach physiologische Chemie an der Universität Bochum. Seit 2003 Gruppenleiter am Max-Planck-Institut für medizinische Forschung Heidelberg und Privatdozent in der Fakultät für Biowissenschaften, Universität Heidelberg.
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Schweizer, R.S., Reinstein, J. Protein-Origami für Fortgeschrittene: Wie DnaK besser falten lernte. Biospektrum 18, 372–375 (2012). https://doi.org/10.1007/s12268-012-0194-8
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DOI: https://doi.org/10.1007/s12268-012-0194-8