2026-07-072026-07-07http://salesiana.dossiersoluciones.com/handle/123456789/17378Scaling of folding times in Go models of proteins and of decoy structures with the Lennard-Jones potentials in the native contacts reveal %robust power law trends when studied under optimal folding conditions. The power law exponent depends on the type of native geometry. Its value indicates lack of kinetic optimality in the model proteins. In proteins, mechanical and thermodynamic stabilities are correlated.REVTex, Proteins: Function, Structure and Genetics - in pressStatistical MechanicsSoft Condensed MatterQuantitative BiologyKinetic non-optimality and vibrational stability of proteinstext