Life in Extreme Environments: How Do the Proteins Work?

Life has been found in many extremes of pressure P, temperature T, and chemical composition X. There are speculations that life on Earth may have originated in deep-sea hydrothermal vents at high P and T and that life on Mars may exist deep subsurface, also at high P and T. This leads to the question of how proteins necessary for life can function at extreme P-T-X. Our focus is mainly on extremes of pressure. First, molecular dynamics simulations of the enzyme dihydrofolate reductase (DHFR) show how P and T affect proteins and how a protein from a piezophile (pressure-loving) is adapted relative to the homologous protein from a mesophile (moderate-loving). Next, molecular dynamics simulations of [4Fe-4S] ferredoxin show how early proteins may have utilized salts in the environment to extend functional control beyond their amino acid sequence, and how P could affect this.

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