Protein folding is a remarkable process leading to molecular recognition in which a random coil with a large number of rapidly interconverting conformers assembles into a unique three- dimensional structure. De novo design, in which attempts to design proteins from scratch, has recently emerged as an attractive approach for investigating this process. The design of proteins often occurs in discrete steps that reflect the hierarchy of forces required for stabilizing tertiary structures. The Principal Investigator has designed several proteins that mimic biophysical properties of natural proteins. He proposes to explore the features of these proteins that give rise to their stable folds, and additionally determine their structures by NMR and X-ray crystallography. He has also prepared helical bundles consisting of right handed and left-handed 1-helices, and proposes to determine their structures by X-ray crystallography. Finally, he proposes to design protein mimetics capable of binding to the activation domains of Ca2+ - calmodulin-dependent enzymes.
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