Quantifying the Chemical Principles of Protein Evolution

A coral’s heat-shock proteins are being studied to reveal the fundamental rules of how proteins evolve. Heat-shock proteins help cells survive stress, but their evolutionary history is poorly understood because their genetic sequences change rapidly. This project examines three forces shaping their evolution: the number of ways a protein can assemble into larger structures (topological entropy), the variety of genetic sequences that produce the same functional protein (sequence entropy), and natural selection. The researchers will sequence heat-shock protein genes from *Porites lutea* corals on Aldabra Atoll, comparing samples from before and after climate-driven bleaching events to see how selection acts alongside entropic constraints. This is fundamental science. It aims to establish whether entropy—a measure of disorder—can drive evolution in the same way natural selection does. If successful, it would provide a quantitative framework for predicting how proteins evolve, not just in corals but across all life. That deeper understanding could eventually help biologists anticipate how organisms adapt to environmental change, or design proteins with predictable evolutionary trajectories for synthetic biology. But the immediate payoff is a clearer picture of evolution’s underlying physical principles.