Researchers Advance Ability To Predict Structures Of Folded Proteins: Computer programs are proving more successful than ever before at calculating structure from amino acid sequence data

A protein is able to perform its biological functions only when the string of amino acids of which it's made has folded up into a compact three-dimensional structure. For many years, scientists have endeavored to understand the process by which protein folding occurs, but success has generally eluded them. The solution to the protein-folding problem is still not at hand and may not be for a long time to come. However, two research groups, working independently, have recently succeeded in developing computational techniques that predict folded protein structures better than ever before. The computer programs developed by the two teams have capabilities that are complementary to each other. A program developed by professor George D. Rose and postdoctoral fellow Rajgopal Srinivasan of the department of biophysics and biophysical chemistry at Johns Hopkins University does an excellent job of predicting protein secondary structure (such as a-helices and â-strands) and supersecondary structure (linked helices a...