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Tensile Mechanics of alpha-Helical Polypeptides
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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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.
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(5) Livadaru, L.; Netz, R. R.; Kreuzer, H. J. Macromolecules 2003, 36, 3732–3744.
Publications
Torabi, K.; Schatz, G. C. Macromolecules Macromolecules, 2013, 46, pp 7947-7956.
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