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(2003 Kuhlman) First design of a protein with a novel backbone topology

Reports the use of 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, with an x-ray crystal structure similar (rms deviation = 1.2 angstroms) to the design model. Much of the deviation occurs in a single exposed loop; little occurs in the protein core.

With link to abstract:

Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D. (2003) “Design of a novel globular protein fold with atomic-level accuracy” Science 302:1364-8.