Abstract
On the ideology of minimalism, we have designed a micro-protein consisting of only 10 amino acids. The molecule, CLN025, exhibits a β-hairpin structure in both crystalline state and aqueous solution. Thermal unfolding is shown to be reversible and can be fitted as a two-state transition. Molecular dynamics simulation starting from an extended conformation leads to a funnel-shaped surface and scale-free network, being the structures located at the bottom and the hub similar to the experimental ones. Considering these consequences, we proposed the concept of “ideal protein” as a way to clarify the differences between “protein” and “peptide”.
