thumb|300px|[[Ribbon diagram of Top7.]]
Top7 is an artificial protein, classified as a de novo protein. This means that the protein itself was designed to have a specific structure and functional properties.
Background
Top7 was designed by Brian Kuhlman and Gautam Dantas in David Baker's laboratory at the University of Washington. Top7's design was built through the use of a general computational method that repeated its sequence design and structure prediction. The end goal was to develop a 93-residue α/β protein with a new sequence and arrangement of its structure, or topology. These computational methods helped to design the proteins along with protein structure prediction algorithms.
Through these analyzes, it was determined that the Top7 protein is extremely stable. Many naturally occurring proteins display cooperative folding, indicating that the whole structure folds in a coordinated procedure. In contrast, the folding of Top7 does not follow a smooth, single phase process. Its non-cooperative characteristic may be linked to its designed sequence, which promotes the formation of an independently folded C-terminal intermediate structure. Studies found that mutations in C-terminal as well as N-terminal of the amino acid sequence of a base model prove that there is a probable sequence of Top7 that allows fold cooperative folding.
Top7 was featured as the RCSB Protein Data Bank's 'Molecule of the Month' in October 2005, and a superposition of the respective cores (residues 60-79) of its predicted and X-ray crystal structures are featured in the Rosetta@home logo.