title: Kinetic nonoptimality and vibrational stability of proteins.
abstract: Scaling of folding times in Go models of proteins and of decoy structures with the Lennard-Jones potentials in the native contacts reveal 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.
authors.affiliation: Institute of Physics, Polish Academy of Sciences, Warsaw, Poland. cieplak@physics.rutgers.edu
authors.forename: M
authors.initials: M
authors.lastname: Cieplak
authors.forename: T X
authors.initials: TX
authors.lastname: Hoang
mesh_terms: D016208:Databases, Factual; D004795:Enzyme Stability / Q000502:physiology; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D014732:Vibration
chemical_list: D011506:Proteins