Abstract
We have developed a statistical mechanical model of the force-extension behavior of α-helical polypeptides, by coupling a random-coil polypeptide elastic model of an inhomogeneous partially freely rotating chain, with the latest version of the helix-coil transition model AGADIR. The model is capable of making quantitatively accurate predictions of force-extension behavior of a given polypeptide sequence including its dependence on pH, temperature and ionic strength. This makes the model a valuable tool for single-molecule protein unfolding experimental studies. Our model predicts the highly reversible unraveling of α-helical structures at small forces of about 20 pN, in good agreement with recent experimental studies.
Original language | English (US) |
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Pages (from-to) | 7947-7956 |
Number of pages | 10 |
Journal | Macromolecules |
Volume | 46 |
Issue number | 19 |
DOIs | |
State | Published - Oct 8 2013 |
ASJC Scopus subject areas
- Organic Chemistry
- Materials Chemistry
- Polymers and Plastics
- Inorganic Chemistry