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Tensile Mechanics of alpha-Helical Polypeptides

By Korosh Torabi1, George C. Schatz1

1. Northwestern University

This model is capable of making quantitatively accurate predictions of force-extension behavior of a given helix-forming polypeptide sequence including its dependence on pH, temperature and ionic strength.

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Version 1.0 - published on 23 Oct 2013

doi:10.4231/D37H1DM78 cite this

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Abstract

This application models the tensile mechanics of a given polypeptide molecule void of tertiary structures. The model includes the effects of the helix formation on force-extension behavior of the polypeptide chain. The model is developed based on the helix-coil transition model AGADIR and iPFRC for the stretching response of the random-coil segments. The quantitatively reliable predictions of this model can supplement a single-molecule protein pulling experiment.

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This work was supported by the Nonequilibrium Energy Research Center (NERC) which is an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC0000989.

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This work was supported by the Nonequilibrium Energy Research Center (NERC) which is an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC0000989.

References

(1) Torabi, K.; Schatz, G. C. Macromolecules Macromolecules, 2013, 46, pp 7947-7956. (1) Muñoz, V.; Serrano, L. Biopolymers 1997, 41, 495-509 (2) Lacroix, E., Viguera AR & Serrano, L. J. Mol. Biol. 1998, 284, 173-191 (3) Hanke, F.; Serr, A.; Kreuzer, H. J.; Netz, R. R. EPL 2010, 92. (24) Livadaru, L.; Netz, R. R.; Kreuzer, H. J. Macromolecules 2003, 36, 3732–3744.

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Torabi, K.; Schatz, G. C. Macromolecules Macromolecules, 2013, 46, pp 7947-7956.

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Researchers should cite this work as follows:

  • Korosh Torabi; George C. Schatz (2013), "Tensile Mechanics of alpha-Helical Polypeptides," https://nanohub.org/resources/ahpull. (DOI: 10.4231/D37H1DM78).

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