Although highly applicable you have to remember evolution is a thing. Proteins where there are no selective pressure to operate at high temperature are likely o

Although highly applicable you have to remember evolution is a thing. Proteins where there are no selective pressure to operate at high temperature are likely optimal in the ranges in that state of water. Hyperthermophiles live at 80degC and above only, they're still made of proteins. Their protein structures are highly similar to other organisms found at lower temperatures, but with modifications such as additional disulphide bonds that increases stability at high temperature. Most of these thermophilic enzymes operate very inefficiently at cooler temperatures or not at all. We already have that sort of broad insight from just looking over evolution and ecological niche. The more interesting thing this finding has to offer is just understanding at a finer detail how proteins interact with water at all, and if there are any properties specific to each state. There might even be cool things like proteins that switch function given the water phase transition. You might find this sort of thing in chaperones related to heat shock for example.