Stretching of proteins in a force-clamp
Piotr Szymczak, Marek Cieplak
Abstract
Mechanically induced protein unfolding in the force-clamp apparatus is shown, in a coarse-grained model of ubiquitin, to have lognormal statistics above a treshold force and exponential below it. Correspondingly, the mean unfolding time is slowly varying and exponentially decreases as a function of the force. The time dependencies of the end-to-end distances are also distinct. The time sequence of unfolding events weakly depends on force and much of it resembles that for stretching at constant speed. A more complicated time dependence arises for integrin.
Create a lesson
Related papers
Reconstruction-Aware Cryo-EM Particle Picking
Riku Itsuji, Yuanhao Wang, Xingjian Li et al.
Dark energy: the cost of function in protein evolution
Ezequiel A. Galpern, Federico Caamaño, Ignacio E. Sánchez et al.
A meta-algorithm for ab initio reconstruction of complex mixtures in cryo-EM
Alkin Kaz, Arda Kaz, Ellen D. Zhong
PHASE: encoding global protein ensembles with local Hamiltonians and all-atom backmapping
Daniele Angioletti, Marco Nobile, Matteo Carli et al.
Analysis of correlations of dwell-times of adjacent kinetic states in the activity of the cold and menthol receptor TRPM8
Ogloblya O. V., Moroz O. F., Zholos A.
Multitask Bayesian Neural Networks for Multiparameter Protein Engineering
Fabio Herrera-Rocha, David Medina-Ortiz, Desiree Wyrzykala et al.