Ronald T. Raines
Departments of Biochemistry and Chemistry
University of Wisconsin
433 Babcock Drive
Madison, WI 53706-1544
1990 Searle Scholar
The amino acid sequence of a protein encodes its three-dimensional structure, and this structure manifests itself in biological function. Using techniques that range from synthetic chemistry to cell biology, we are illuminating in atomic detail both the chemical basis and the biological purpose for protein structure and protein function. Our work now focuses on the following problems.
Protein FunctionWe are revealing the molecular basis for the special biological activities of two ribonucleases: onconase (which is toxic to tumor cells) and angiogenin (which promotes neovascularization). In addition, we are using nucleases to reveal fundamental insights into enzymatic catalysis (including processivity) and protein - nucleic acid interactions.
Protein FoldingFoldases catalyze the folding of other proteins. We are designing and creating new protein and small-molecule foldases that catalyze the formation of native disulfide bonds in vitro and in vivo.
Protein StabilityCollagen, the most abundant protein in animals, is a simple protein with impressive stability. By using synthetic collagen mimics, we are determining the contribution of hydrogen bonds and stereoelectronic effects to this stability. Our mimics may provide new materials for tissue welding and other medical procedures.
Protein - Protein InteractionsWe are using novel genetic selections and screens to identify molecules from combinatorial libraries that inhibit the dimerization of HIV-1 protease or other proteins of therapeutic interest.
Our efforts are leading to insights into the relationship between amino acid sequence and protein function (or dysfunction), as well as to the creation of novel molecules with desirable properties.
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