Conformational entropy is a concept from thermodynamics and statistical mechanics that refers to the number of different ways a molecule can arrange itself in space while maintaining its overall structure. It is a key component of the free energy of a system and plays a significant role in determining the stability and reactivity of molecular systems. In more technical terms, conformational entropy quantifies the diversity of conformations (the various spatial arrangements of atoms in a molecule) available to a given molecular system.
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Conformational entropy measures the multiplicity of molecular conformations compatible with specified macroscopic constraints. For equally weighted accessible conformations it is ; for probabilities , it is . A folded protein generally has less chain conformational entropy than its unfolded ensemble, but folding can still lower total Gibbs free energy when solvent and interaction contributions are included.