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Protein Forced Unfolding and Its Effects on the Finite Deformation Stress-Strain Behavior of Biomacromolecular Solids

Published online by Cambridge University Press:  01 February 2011

H. Jerry Qi
Affiliation:
Departments of Mechanical Engineering Massachusetts Institute of Technology, Cambridge, MA 02139 Department of Mechanical Engineering, University of Colorado, Boulder, CO 80309
Christine Ortiz
Affiliation:
Materials Science and Engineering
Mary C. Boyce
Affiliation:
Departments of Mechanical Engineering
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Abstract

Many proteins have been experimentally observed to exhibit a force-extension behavior with a characteristic repeating pattern of a nonlinear rise in force with imposed displacement to a peak, followed by a significant force drop upon reaching the peak (a “saw-tooth” profile) due to successive unfolding of modules during extension. This behavior is speculated to play a governing role in biological and mechanical functions of natural materials and biological networks composed of assemblies of such protein molecules. In this paper, a constitutive model for the finite deformation stress-strain behavior of crosslinked networks of modular macromolecules is developed. The force-extension behavior of the individual modular macromolecule is represented using the Freely Jointed Chain (FJC) statistical mechanics model together with a two-state theory to capture unfolding. The single molecule behavior is then incorporated into a formal continuum mechanics framework to construct a constitutive model. Simulations illustrate a relatively smooth “yield”-like stress-strain behavior of these materials due to activate unfolding in these microstructures.

Type
Research Article
Copyright
Copyright © Materials Research Society 2005

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References

[1] Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J.M., Gaub, H.E., Science, 276, 1109 (1997).Google Scholar
[2] Oberhauser, A.F., Marszalek, P.E., Erickson, H.P., Fernandez, J.M., Nature, 393, 181 (1998).Google Scholar
[3] Law, R., Carl, P., Harper, S., Dalhaimer, P., Speicher, D., Discher, D.E., Biophys. J., 84, 533 (2003).Google Scholar
[4] Kuhn, W., Grun, F., Kolliod Z., 101, 248 (1942).Google Scholar
[5] Bell, G.I., Science, 200, 618 (1978).Google Scholar
[6] Evans, E., Ritchie, K., Biophys. J., 72, 1541 (1997).Google Scholar
[7] Improta, S., Politou, A.S., Pastore, A., Structure, 4, 323 (1996).Google Scholar
[8] Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., Nucleic Acids Research, 28, 235 (2000).Google Scholar
[9] Rief, M., Fernandez, J.M., Gaub, H.E.. Phys. Rev. Let., 81, 4764 (1998).Google Scholar
[10] Arruda, E.M., Boyce, M.C., J. Mech. Phys. Solids, 41, 389 (1993).Google Scholar
[11] Becker, N., Oroudjev, E., Mutz, S., Cleveland, J.P., Hansma, P.K., Hayashi, C.Y., Makarov, D.E., H.G. Hansma. 21, 278 (2003).Google Scholar
[12] Qi, H.J., Ortiz, C., Boyce, M.C.; Proceedings of IUTAM, Springer Verlag, ed. Holzapfel, G. and Ogden, R.W. (2005).Google Scholar