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Biophys. J. BioFAST: First Published December 15, 2006. doi:10.1529/biophysj.106.101261
© 2006 by the Biophysical Society.

A more recent version of this article appeared on March 1, 2007.
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BIOPHYSICAL LETTERS

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM

Andre E. X. Brown 1, Rustem I. Litvinov 1, Dennis E. Discher 1 and John W Weisel 2*

1 University of Pennsylvania
2 University of Pennsylvania School of Medicine

* To whom correspondence should be addressed. E-mail: weisel{at}mail.med.upenn.edu.

Submitted on November 15, 2006
Revised on December 1, 2006
Accepted on 11 December 2006


  Abstract
Fibrinogen is a blood plasma protein that, after activation by thrombin, assembles into fibrin fibers that form the elastic network of blood clots. We used atomic force microscopy (AFM) to study the forced unfolding of engineered linear oligomers of fibrinogen, and we show that forced extension of the oligomers produces sawtooth patterns with a peak-to-peak length consistent with the independent unfolding of the coiled-coils in a cooperative two-state manner. In contrast with force plateaus seen for myosin coiled-coils that suggested rapid refolding of myosin, Monte Carlo simulations of fibrinogen unfolding confirm that fibrinogen refolding is negligible on experimental time scales. The distinct behavior of fibrinogen seems to be due to its topologically complex coiled-coils and an interaction between fibrinogen's {alpha}C-domains and its central region.

Key Words: atomic force microscopy, coiled coil, fibrin blood clot, fibrinogen, single molecule, unfolding




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E. Bura, D. K. Klimov, and V. Barsegov
Analyzing Forced Unfolding of Protein Tandems by Ordered Variates, 2: Dependent Unfolding Times
Biophys. J., April 1, 2008; 94(7): 2516 - 2528.
[Abstract] [Full Text] [PDF]


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Copyright © 2006 by the Biophysical Society.