Stretching of Proteins in the Entropic Limit

Abstract

Mechanical stretching of six proteins is studied through molecular dynamics simulations. The model is Go-like, with Lennard-Jones interactions at native contacts. Low temperature unfolding scenarios are remarkably complex and sensitive to small structural changes. Thermal fluctuations reduce the peak forces and the number of metastable states during unfolding. The unfolding pathways also simplify as temperature rises. In the entropic limit, all proteins show a monotonic decrease of the extension where bonds rupture with their separation along the backbone (contact order).

RevTex, 5 pages, 5 figures, to appear in Phys. Rev. E

References in corpus (2)

• Universality classes in folding times of proteins
• Folding Pathways of Prion and Doppel

Cited by in corpus (7)

• Dodging the crisis of folding proteins with knots
• How knots influence properties of proteins
• Inferring the diameter of a biopolymer from its stretching response
• Mechanical properties of the domains of titin in a Go-like model
• Thermal unfolding of proteins
• Mechanical Stretching of Proteins: Calmodulin and Titin
• Thermal effects in stretching of Go-like models of titin and secondary structures