The elastic free energy of a tandem modular protein under force

Jessica Valle-Orero, Edward C. Eckels, Guillaume Stirnemann, Ionel Popa, Ronen Berkovich, Julio M. Fernandez

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Recent studies have provided a theoretical framework for including entropic elasticity in the free energy landscape of proteins under mechanical force. Accounting for entropic elasticity using polymer physics models has helped explain the hopping behavior seen in single molecule experiments in the low force regime. Here, we expand on the construction of the free energy of a single protein domain under force proposed by Berkovich et al. to provide a free energy landscape for N tandem domains along a continuous polypeptide. Calculation of the free energy of individual domains followed by their concatenation provides a continuous free energy landscape whose curvature is dominated by the worm-like chain at forces below 20 pN. We have validated our free energy model using Brownian dynamics and reproduce key features of protein folding. This free energy model can predict the effects of changes in the elastic properties of a multidomain protein as a consequence of biological modifications such as phosphorylation or the formation of disulfide bonds. This work lays the foundations for the modeling of tissue elasticity, which is largely determined by the properties of tandem polyproteins.

Original languageEnglish
Pages (from-to)434-438
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume460
Issue number2
DOIs
StatePublished - 1 May 2015

Keywords

  • Force spectroscopy
  • Free energy landscape
  • Langevin dynamics
  • Protein folding
  • Tandem modular protein
  • Tissue elasticity

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