Adaptation of Proteins: Nature Plus Nurture

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Somero 9727721 Understanding how temperature-sensitive proteins are stabilized in organisms that experience widely different temperatures has significance for both basic and applied science. The PIs will examine two types of changes that play major roles in temperature adaptation. First, changes in amino acid sequences of proteins (their "nature") will be investigated. By determining where adaptive substitutions occur in proteins of differently thermally-adapted species, the PIs will gain a deeper understanding of how specific alterations of protein sequence affect the molecules' structure and function, and how these adaptive changes help to establish environmental tolerance limits. Temperature changes of only a few degrees centigrade are adequate to perturb proteins and affect organismal distribution patterns-a finding with clear implications for models of global warming. Furthermore, an understanding of how evolutionary processes alter protein stability will assist biotechnologists in developing strategies for laboratory-engineering of protein stability. Protein stability is also influenced by the small molecules and water that bathe proteins in cells. The PIs will investigate how the aqueous medium in which a protein functions helps to "nurture" the protein to enhance stability. Discovery of novel stabilizing solutes could facilitate development by biotechnologists of new types of solutions for the long-term, safe storage of drugs, cells, and tissues.