Format

Send to

Choose Destination
See comment in PubMed Commons below
Biophys J. 2007 Mar 1;92(5):L39-41. Epub 2006 Dec 15.

Forced unfolding of coiled-coils in fibrinogen by single-molecule AFM.

Author information

1
Department of Physics and Astronomy, Nano/Bio Interface Center, University of Pennsylvania, Philadelphia, Pennsylvania, USA.

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 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 timescales. The distinct behavior of fibrinogen seems to be due to its topologically complex coiled-coils and an interaction between fibrinogen's alphaC-domains and its central region.

PMID:
17172299
PMCID:
PMC1796812
DOI:
10.1529/biophysj.106.101261
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center