Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

Details Design of a Novel Globular Protein Fold with Atomic-Level Accuracy Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

Nov 2003

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2003sci...302.1364k&link_type=abstract

Science, Volume 302, Issue 5648, pp. 1364-1368 (2003).

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Scientific paper

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 α/β 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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