Protein design opens new ways to probe the determinants of folding and to facilitate the study of protein function. Such design is complicated, however, by the conformational complexity of proteins and by the large numbers of possible sequences. Recent computational methods for identifying the properties of amino acid sequences likely to fold to a given three-dimensional structure will be presented, as will several examples of structures so designed, which have been experimentally synthesized and characterized. The roles of water and solvation in the folding of proteins and nonbiological foldamers will also be discussed.
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