A Thermodynamic Model for Prebiotic Protein Function

We propose a scenario for the prebiotic co-evolution of RNA and of fast folding proteins with large entropy gaps as observed today. We show from very general principles that the folding and unfolding of the proteins synthesized by RNA can function as a heat pump. Rock surfaces can facilitate the folding of amino acid chains having polar and hydrophobic residues, with an accompanying heat loss to the surrounding rock. These chains then absorb heat from the soup as they unfold. This opens the way to the enhancement of RNA replication rates, by the enzymatic action of folded proteins present in greater numbers at reduced temperatures. This gives an evolutionary advantage to those RNA coding amino acid sequences with non-degenerate folded states which would provide the most efficient refrigeration.