Abstract
A research team has designed, assembled, and characterized a synthetic protein whose size, complexity, and folding pattern closely resemble those of natural proteins. The protein's 73 residues, which include 19 of the 20 types of naturally occurring amino acids, form three α-helices that interact with each other through hydrophobic contacts closely resembling those found in many biological proteins. The accomplishment—by biochemistry and biophysics professor William F. DeGrado and graduate student Scott T. R. Walsh of the University of Pennsylvania, senior member Heinrich Roder of Fox Chase Cancer Center, Philadelphia, and coworkers—suggests that the ability to design proteins to order for specific functional tasks may not be that far off [ Proc. Natl. Acad. Sci. USA , 96 , 5486 (1999)] The synthetic protein, called oc3D, has a well-packed hydrophobic core and a number of other structural, thermodynamic, and spectroscopic characteristics typical of natural proteins. Hydrophobic cores are key structural fe...
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