Controlled Assembly of the Filamentous Chaperone Gamma-Prefoldin into Defined Nanostructures

  • Douglas S. Clark
  • Dominic J. Glover
Part of the Methods in Molecular Biology book series (MIMB, volume 1798)


Self-assembling protein templates have enormous potential for the fabrication of multifunctional nanostructures that require precise positioning of individual molecules, such as enzymes and inorganic moieties, in regular patterns. A recently described approach uses ultrastable filaments composed of the gamma-prefoldin (γPFD) protein and engineered connector proteins to construct novel architectures useful for basic research and practical applications in nanobiotechnology. Here we describe the production of the γPFD and connector proteins from E. coli, and the assembly of γPFD with connector proteins into macromolecular structures with defined shapes.

Key words

Filament Protein Self-assembly Biomaterials Prefoldin Template Nanomaterials 



We are grateful to Samuel Lim for reviewing the manuscript and making helpful suggestions. This work was supported by the Air Force Office of Scientific Research (FA9550-14-1-0026).


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Chemical and Biomolecular EngineeringUniversity of CaliforniaBerkeleyUSA
  2. 2.School of Biotechnology and Biomolecular SciencesThe University of New South WalesSydneyAustralia

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