AFM Force Spectroscopy and Steered Molecular Dynamics Simulation of Protein Contactin 4
J. Strzelecki a, K. Mikulska a, M. Lekka b, A. Kulik c, A. Balter a and W. Nowak a
a Institute of Physics, Nicolaus Copernicus University, Grudziądzka 5, 87-100 Toruń, Poland
b The Henryk Niewodniczanski Institute of Nuclear Physics, Polish Academy of Sciences, Radzikowskiego 152, 31-342 Kraków, Poland
c Institute of Physics of Complex Matter, Ecole Polytechnique Federale de Lausanne, Ch-1015 Lausanne, Switzerland
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We use a single molecule atomic force spectroscopy combined with the steered molecular dynamics simulation to determine a mechanical behavior of neural cell adhesion protein contactin during its unfolding. Force curves typical for modular proteins were observed, showing at most four unfolding peaks. The analysis of force spectra performed within worm-like chain model of polymer elasticity showed the presence of three unfolding lengths. Small plateaus, most likely resulting from forced transitions within domains were observed for the first time. Steered molecular dynamics simulations help to determine atomistic picture of domain unfolding.
DOI: 10.12693/APhysPolA.116.S-156
PACS numbers: 82.37.Rs, 87.10.Tf