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PEDS Advance Access published online on August 27, 2004
Protein Engineering Design and Selection, doi:10.1093/protein/gzh069
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Received March 29, 2004
Revised June 24, 2004
Accepted August 12, 2004

Short Communication

A thermo-stable enzyme as an experimental platform to study properties of less stable homologues

Holger Lill 1, Toru Hisabori 2, Georg Groth 3, Dirk Bald 1*

1 Department of Structural Biology, Faculty of Earth- and Life Science, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands
2 Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan
3 Department of Plant Biochemistry, University of Duesseldorf, Universitaetsstrasse1, 40225 Duesseldorf, Germany

* To whom correspondence should be addressed. E-mail: dirk.bald{at}falw.vu.nl.


  Abstract

Structural and functional characterization of proteins is frequently hampered by lack of stability or by insufficient assembly of oligomeric proteins in over-expression systems. Using F1-ATPase as a case study we here tackle this problem by introducing function determining domains from a difficult-to-handle variety of an enzyme into a stable homologue.

Keywords: Protein stability; protein assembly; protein engineering; chimeric enzyme.
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