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

Science (New York, N.Y.) | Nov 21, 2003

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.

Pubmed ID: 14631033 RIS Download

Mesh terms: Algorithms | Amino Acid Sequence | Circular Dichroism | Computational Biology | Computer Graphics | Computer Simulation | Crystallization | Crystallography, X-Ray | Databases, Protein | Models, Molecular | Molecular Sequence Data | Monte Carlo Method | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Protein Denaturation | Protein Engineering | Protein Folding | Protein Structure, Secondary | Proteins | Software | Solubility | Temperature | Thermodynamics