Tensile Mechanics of α‑Helical Polypeptides
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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