Abstract
This work is aimed at determining the energy-level statistics of the fine resolution of soft-mode dynamics warranting an adiabatically simplified structural relaxation of a folding biopolymer chain. The parameters defining the intrabasin structure relaxation are specified for RNA, so that each Watson-Crick base-pairing pattern may be treated as a quasiequilibrium ensemble of substates or torsional isomers within relevant folding time scales. The temperature-dependent threshold for energy dispersion associated with the fine structure of each superbasin is determined so as to warrant the adiabatic entrainment of the torsional dynamics.
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