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Protein structure: Has Levinthal's paradox “folded”?

An annual competition among computational biochemists is held by an organization called Critical Assessment of Protein Structure Prediction (CASP). The winning 2020 entrant was from DeepMind, a British machine learningbased company. This team tweaked their earlier work into a refinement that outpaced not only the competing platforms but also previous efforts in this mode of the protein folding field. The notion that linear arrays of amino acids function because of the polymer's folded structure arose early in the protein field.1,2 Key early discoveries were made by Alfred Mirsky (Figure 1) and later by Christian Anfinsen (Figure 2). These pioneering experiments demonstrated that amino acid side chain interactions dictated the final structure, epistemologically erasing a previous era in which zephyrs of vitalism still were at play, and the structure of proteins, whether colloids, glob(ule)s, or whatever was shrouded in mystery. Once the biochemistry of protein biosynthesis had been established in the 1950s, a few astute biochemists recognized that the nascent polypeptide chain might start to fold before it had been finished, while others (the majority) focused on how the final product would fold. There was empirical work, some of it hapless but much instructive, and yet it seemed clear that the problem's combinatorial dimension was a great challenge; perhaps a better adjective was “astonishing.” Another term used by some at the time was “unsolvable.” Sometimes it takes an oddball to move things in science, and I would contend that the molecular biologist Cyrus Levinthal was one (Figure 3) and that he did that. In 1969, he published the notion that a typical protein could have something like 10300 possible conformations, and he quipped that solving them all would take longer than the age of the universe.3 In his subsequent career, he put all his formidable scientific energy into applying computer science to biochemistry