2020 年 60 巻 6 号 p. 325-330
Protein design holds promise for applications such as control of cells, therapeutics, new enzymes and protein-based materials. Recently, rational design of protein molecules has made a great progress, guided by the consistency principle proposed by Nobuhiro Gō in 1983: local and non-local interactions consistently favor the same folded conformation. We discovered a set of rules for designing ideal protein structures stabilized by consistent local and non-local interactions. The rules enabled the de novo design of amino acid sequences having the funnel-shaped energy landscapes toward the desired target structures. Various ideal protein structures have been created using the rules.