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Design of a novel globular protein fold with atomic-level accuracy.

Authors:
Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D
Affiliation:
Journal:
Science (New York, N.Y.)

Abstract

A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature.

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