Repository logo
 

Non-exponential kinetics of unfolding under a constant force

Accepted version
Peer-reviewed

Type

Article

Change log

Authors

Terentjev, EM 

Abstract

We examine the population dynamics of naturally folded globular polymers, with a super-hydrophobic "core" inserted at a prescribed point in the polymer chain, unfolding under an application of external force, as in AFM force-clamp spectroscopy. This acts as a crude model for a large class of folded biomolecules with hydrophobic or hydrogen-bonded cores. We find that the introduction of super-hydrophobic units leads to a stochastic variation in the unfolding rate, even when the positions of the added monomers are fixed. This leads to the average non-exponential population dynamics, which is consistent with a variety of experimental data and does not require any intrinsic quenched disorder that was traditionally thought to be at the origin of non-exponential relaxation laws.

Description

Keywords

Biopolymers, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Kinetics, Microscopy, Atomic Force, Models, Molecular, Molecular Conformation, Protein Unfolding, Stochastic Processes, Ubiquitin

Journal Title

The Journal of Chemical Physics

Conference Name

Journal ISSN

0021-9606
1089-7690

Volume Title

145

Publisher

AIP Publishing
Sponsorship
Engineering and Physical Sciences Research Council (EP/J017639/1)
This work is supported by the EPSRC through a studentship award and the Critical Mass Grant for Cambridge Theoretical Condensed Matter EP/J017639.