Pathways of mechanical unfolding of FnIII_{10}: low force intermediates

Abstract

We study the mechanical unfolding pathways of the $FnII{I}_{10}$ domain of fibronectin by means of an Ising--like model, using both constant force and constant velocity protocols. At high forces and high velocities our results are consistent with experiments and previous computational studies. Moreover, the simplicity of the model allows us to probe the biologically relevant low force regime, where we predict the existence of two intermediates with very close elongations. The unfolding pathway is characterized by stochastic transitions between these two intermediates.

References in corpus (13)

• Exact Solution of the Munoz-Eaton Model for Protein Folding
• An Ising-Like model for protein mechanical unfolding
• Effects of intermediate bound states in dynamic force spectroscopy
• Mechanical unfolding and refolding pathways of ubiquitin
• Changing the mechanical unfolding pathway of FnIII10 by tuning the pulling strength
• Kinetics of the Wako-Saito-Munoz-Eaton Model of Protein Folding
• Downhill versus two-state protein folding in a statistical mechanical model
• Protein mechanical unfolding: a model with binary variables
• Rate Determining Factors in Protein Model Structures
• Exactness of the cluster variation method and factorization of the equilibrium probability for the Wako-Saito-Munoz-Eaton model of protein folding
• Rigorous results on the local equilibrium kinetics of a protein folding model
• Unfolding times for proteins in a force clamp
• Equilibrium properties and force-driven unfolding pathways of RNA molecules

Cited by in corpus (4)

• Analysis of the Equilibrium and Kinetics of the Ankyrin Repeat Protein Myotrophin
• Direction dependent mechanical unfolding and Green Fluorescent Protein as a force sensor
• Effects of confinement on thermal stability and folding kinetics in a simple Ising-like model
• Nonequilibrium dynamics of an exactly solvable Ising-like model and protein translocation