Tensile mechanics of α-helical polypeptides

Korosh Torabi, George C Schatz

Research output: Contribution to journalArticle

5 Citations (Scopus)

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 languageEnglish
Pages (from-to)7947-7956
Number of pages10
JournalMacromolecules
Volume46
Issue number19
DOIs
Publication statusPublished - Oct 8 2013

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Polypeptides
Mechanics
Peptides
Ionic strength
Proteins
Molecules

ASJC Scopus subject areas

  • Organic Chemistry
  • Materials Chemistry
  • Polymers and Plastics
  • Inorganic Chemistry

Cite this

Tensile mechanics of α-helical polypeptides. / Torabi, Korosh; Schatz, George C.

In: Macromolecules, Vol. 46, No. 19, 08.10.2013, p. 7947-7956.

Research output: Contribution to journalArticle

Torabi, Korosh ; Schatz, George C. / Tensile mechanics of α-helical polypeptides. In: Macromolecules. 2013 ; Vol. 46, No. 19. pp. 7947-7956.
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