Thermal unfolding of proteins

Abstract

Thermal unfolding of proteins is compared to folding and mechanical stretching in a simple topology-based dynamical model. We define the unfolding time and demonstrate its low-temperature divergence. Below a characteristic temperature, contacts break at separate time scales and unfolding proceeds approximately in a way reverse to folding. Features in these scenarios agree with experiments and atomic simulations on titin.

3 figures, a text in latex

References in corpus (5)

• Folding Kinetics of Protein Like Heteropolymers
• Universality classes in folding times of proteins
• Mechanical properties of the domains of titin in a Go-like model
• Lattice tube model of proteins
• Stretching of Proteins in the Entropic Limit

Cited by in corpus (7)

• How knots influence properties of proteins
• Cotranslational folding of deeply knotted proteins
• Molecular jamming - the cystine slipknot mechanical clamp in all-atom simulations
• Effects of confinement and crowding on folding of model proteins
• Citrate synthase proteins in extremophilic organisms: Studies within a structure-based model
• Re-equilibration after quenches in athermal martensites:Conversion-delays for vapour to liquid domain-wall phases
• Golf-course and funnel energy landscapes: Protein folding concepts in martensites