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Biophys. J. BioFAST: First Published December 8, 2006. doi:10.1529/biophysj.106.097741
© 2006 by the Biophysical Society.

A more recent version of this article appeared on February 15, 2007.
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PROTEINS

The Mechanical Fingerprint of a Parallel Polyprotein Dimer

Atom Sarkar 1*, Sofia Caamano 2 and Julio M. Fernandez 2

1 The Ohio State University Medical Center
2 Columbia University

* To whom correspondence should be addressed. E-mail: atom.sarkar{at}osumc.edu.

Submitted on October 12, 2006
Revised on November 9, 2006
Accepted on 22 November 2006


  Abstract
We use the GCN4 oligomerization domain to engineer a covalently linked parallel polyprotein dimer based on the well studied I27 domain of titin. We use single molecule AFM techniques to stretch single polyprotein fibers and verify their mechanical properties. We find that the engineered polyprotein dimers extend in perfect register, doubling the unfolding force and halving the persistence length without changing the increase in contour length. These experiments directly confirm the mechanical scaling laws proposed for parallel bundles of modular proteins.

Key Words: GCN4, I27, atomic force spectroscopy, polyprotein, single molecule




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A. F. Oberhauser and M. Carrion-Vazquez
Mechanical Biochemistry of Proteins One Molecule at a Time
J. Biol. Chem., March 14, 2008; 283(11): 6617 - 6621.
[Abstract] [Full Text] [PDF]


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Copyright © 2006 by the Biophysical Society.