Thermodynamics of protein folding: a random matrix formulation

摘要

The process of protein folding from an unfolded state to a biologicallyactive, folded conformation is governed by many parameters e.g the sequence ofamino acids, intermolecular interactions, the solvent, temperature and chaperonmolecules. Our study, based on random matrix modeling of the interactions,shows however that the evolution of the statistical measures e.g Gibbs freeenergy, heat capacity, entropy is single parametric. The information canexplain the selection of specific folding pathways from an infinite number ofpossible ways as well as other folding characteristics observed in computersimulation studies.