Kinetic non-optimality and vibrational stability of proteins

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dc.creatorCieplak, Marek
dc.creatorHoang, Trinh Xuan
dc.date2001-02-18
dc.date.accessioned2026-07-25T14:18:04Z
dc.descriptionScaling 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.
dc.descriptionREVTex, Proteins: Function, Structure and Genetics - in press
dc.identifierhttps://arxiv.org/abs/cond-mat/0102316
dc.identifierhttp://arxiv.org/abs/cond-mat/0102316
dc.identifier.urihttps://dspace.dare.co.zw/handle/123456789/24601
dc.subjectStatistical Mechanics
dc.subjectSoft Condensed Matter
dc.subjectQuantitative Biology
dc.titleKinetic non-optimality and vibrational stability of proteins
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