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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

This tool is closed source.



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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.

Tags, a resource for nanoscience and nanotechnology, is supported by the National Science Foundation and other funding agencies. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation.