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Protein folding and design are major biophysical problems, the solution ofwhich would lead to important applications especially in medicine. Here a novelprotein model capable of simultaneously provide quantitative protein design andfolding is introduced. With computer simulations it is shown that, for a largeset of real protein structures, the model produces designed sequences withsimilar physical properties to the corresponding natural occurring sequences.The designed sequences are not yet fully realistic and require furtherexperimental testing. For an independent set of proteins, notoriously difficultto fold, the correct folding of both the designed and the natural sequences isalso demonstrated. The folding properties are characterized by free energycalculations. which not only are consistent among natural and designedproteins, but we also show a remarkable precision when the folded structuresare compared to the experimentally determined ones. Ultimately, this novelcoarse-grained protein model is unique in the combination of its fundamentalthree features: its simplicity, its ability to produce natural foldabledesigned sequences, and its structure prediction precision. The latterdemonstrated by free energy calculations. It is also remarkable that lowfrustration sequences can be obtained with such a simple and universal designprocedure, and that the folding of natural proteins shows funnelled free energylandscapes without the need of any potentials based on the native structure.

Transferable coarse-grained potential for $\textit{de novo}$ protein folding and design