Figures and Tables
From the following article:
The molecular elasticity of the extracellular matrix protein tenascin
Andres F. Oberhauser, Piotr E. Marszalek, Harold P. Erickson and Julio M. Fernandez
Nature 393, 181-185(14 May 1998)
doi:10.1038/30270
Figure 1
Force–extension relationships for native tenascin hexabrachions measured with AFM techniques.
Full size figure and legend (35K)
Figure 2
The WLC model, using a persistence length of p = 0.42 nm and a contour length increment of 
lc = 28.5 nm, describes the force–extension curves of recombinant tenascin fragments.
Figure 3
Repeated unfolding/refolding cycles of a single recombinant TNfnALL protein.
Full size figure and legend (35K)
Figure 4
Repeated refolding cycles of a single TNfnAll protein using a double-pulse experiment (inset) identifies at least two refolding rate constants.
Full size figure and legend (37K)
Figure 5
A Monte Carlo simulation shows that tandem FN-III repeats can extend the range and lifetime of a protein–ligand bond and reduce the force required to break it (see Methods).
Full size figure and legend (45K)