Top7

[1] Top7 was designed by Brian Kuhlman and Gautam Dantas in David Baker's laboratory at the University of Washington.

In order to achieve a target structure, researchers first developed a two-dimensional diagram and utilized it to determine the constraints that allowed them to construct the three-dimensional model of Top7.

It was also discovered that an increase in temperature allows the protein to unfold cooperatively and displays cold denaturation.

Its non-cooperative characteristic may be linked to its designed sequence, which promotes the formation of an independently folded C-terminal intermediate structure.

This has broad implications for advancing the field of computational protein design and provides a platform for the creation of novel biomolecules with desired properties.

Understanding these principles can contribute to the development of more stable and functional proteins not derived from natural evolution.