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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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Archive Version 1.0
Published on 23 Oct 2013
Latest version: 1.1. All versions

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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