AFM Force Spectroscopy and Steered Molecular Dynamics Simulation of Protein Contactin 4

• Authors: J. Strzelecki
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

82.37.Rs; 87.10.Tf

Discipline

• 82.37.Rs: Single molecule manipulation of proteins and other biological molecules
• 87.10.Tf: Molecular dynamics simulation

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2009
• Volume: 116
• Issue: S
• Pages: S-156-S-159

Dates

published

2009-12

Contributors

author

J. Strzelecki

• Institute of Physics, Nicolaus Copernicus University, Grudziądzka 5, 87-100 Toruń, Poland

References

• 1. T. Kaneko-Goto, S. Yoshihara, H. Miyazaki, Y. Yoshihara, Neuron 57, 834 (2008)
• 2. T. Fernandez, T. Morgan, N. Davis, A. Klin, A. Morris, A. Farhi, R.P. Lifton, M.W. State, Am. J. Human Gen. 74, 1286 (2004)
• 3. J. Roohi, C. Montagna, D.H. Tegay, L.E. Palmer, C. DeVincent, J.C. Pomeroy, S.L. Christian, N. Nowak, E. Hatchwell, J. Med. Genet. 46, 176 (2009)
• 4. G. Binnig, C.F. Quate, C. Gerber, Phys. Rev. Lett. 56, 930 (1986)
• 5. E.L. Florin, V.T. Moy, H.E. Gaub, Science 264, 415 (1994)
• 6. H. Clausen-Schaumann, M. Rief, C. Tolksdorf, H.E. Gaub, Biophys. J. 78, 1997 (2000)
• 7. P.E. Marszalek, A.F. Oberhauser, Y.P. Pang, J.M. Fernandez, Nature 396, 661 (1998)
• 8. G. Lee, W. Nowak, J. Jaroniec, Q. Zhang, P.E. Marszalek, Biophys. J. 87, 1456 (2004)
• 9. M. Rief, M. Gautel, F. Oesterhelt, J.M. Fernandez, H.E. Gaub, Science 276, 1109 (1997)
• 10. G. Lee, K. Abdi, Y. Jiang, P. Michaely, V. Bennett, P. Marszalek, Nature 440, 246 (2006)
• 11. K. Lebed, M. Lekka, J. Lekki, W.M. Kwiatek, A. Dabrowska, J. Phys. Condens. Matter 18, 10157 (2006)
• 12. J. Roohi, C. Montagna, D.H. Tegay, L.E. Palmer, C. DeVincent, J.C. Pomeroy, S.L. Christian, N. Nowak, E. Hatchwell, Brit. Med. J. 336, 414 (2008)
• 13. M. Rabbi, P.E. Marszalek, Cold Spring Harbor Protocols 2007, pdb.prot4899, 2007
• 14. J.L. Hutter, J. Bechhoefer, Rev. Sci. Instrum. 64, 1868 (1993)
• 15. C. Bustamante, J.F. Marko, E.D. Siggia, S.B. Smith, Science 265, 1599 (1994)
• 16. M.T. Nelson, W. Humphrey, A. Gursoy, A. Dalke, L.V. Kale, R.D. Skeel, K. Schulten, Int. J. High Perform. Comput. Appl. 10, 251 (1996)
• 17. T. Schwede, J. Kopp, N. Guex, M.C. Peitsch, Nucleic Acids Res. 31, 3381 (2003)
• 18. W. Nowak, P. Marszalek, in: Current Trends in Computational Chemistry, Ed. J. Leszczyński, World Scientific, Singapore 2005
• 19. W. Humphrey, A. Dalke, K. Schulten, J. Mol. Graph. 14, 33 (1996)
• 20. A.P. Wiita, S.R.K. Ainavarapu, H.H. Huang, J.M. Fernandez, Proc. Nat. Acad. Sci. 103, 7222 (2006)
• 21. P. Marszalek, H. Lu, H. Li, M. Carrion-Vazquez, A. Oberhauser, K. Schulten, J. Fernandez, Nature 402, 100 (1999)

Identifiers

DOI

10.12693/APhysPolA.116.S-156