 The conformational entropy associated with a particular structure or state, such as an alpha-helix, a folded or an unfolded protein structure, is then dependent on the probability of the occupancy of that structure.The entropy of heterogeneous random coil or denatured proteins is significantly higher than that of the folded native state tertiary structure.In particular, the conformational entropy of the amino acid side chains in a protein is thought to be a major contributor to the energetic stabilization of the denatured state and thus a barrier to protein folding.