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Originally published as Biophys J. BioFAST on December 8, 2006.
doi:10.1529/biophysj.106.097741
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Biophysical Journal 92:L36-L38 (2007)
© 2007 The Biophysical Society

The Mechanical Fingerprint of a Parallel Polyprotein Dimer

Atom Sarkar, Sofia Caamano and Julio M. Fernandez

Department of Biological Sciences, Columbia University, New York, New York 10027

Correspondence: Address reprint requests and inquiries to Atom Sarkar, E-mail: atom.sarkar{at}osumc.edu; or Julio M. Fernandez, E-mail: jfernandez{at}columbia.edu.

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 atomic force microscopy 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 while keeping the contour length increase unchanged. These experiments directly confirm the mechanical scaling laws proposed for parallel bundles of modular proteins.




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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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