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A review from the group leading recent rapid progress in de novo protein design describes the successes, identifies the remaining challenges, and heralds the advance “from the Stone Age to the Iron Age” in protein design.
Computer designed networks of hydrogen bonds allow programming specific interactions of protein interfaces, facilitating programming molecular recognition.
Computational design of an enzyme that carboligates three one-carbon molecules to form one three-carbon molecule, an activity that does not exist in nature, provides proof-of-principle for a novel metabolic pathway for carbon fixation.
New families of protein structures, barrel proteins for positioning small molecules, self-assembling protein arrays, and precision sculpting of protein architectures highlight de novo protein design advances.
A fully automated design protocol generates dozens of designs for proteins based on helix-loop-helix-loop repeat units that are very stable, have crystal structures that match the design, have very different overall shapes, and are unrelated to any natural protein.
Foldit game players have again out-performed scientists in protein design, this time improving the design of a protein designed from scratch to catalyze Diels-Alder cycloadditions.
Engineered bacteria that incorporate unnatural amino acids at multiple positions provide a new tool that may facilitate designing proteins to fold more predictably into molecular machinery components.
Scientists at the University of Pennsylvania used basic engineering principles derived from studying natural proteins to design from scratch a simple and small protein that performed the function of carrying oxygen that is performed by natural globin proteins.
New computational results reveal how the proper hierarchical assembly of smaller protein domains optimizes mechanical properties.
Can online gamers add to the nanotech toolkit for perfecting the de novo design of proteins that do not exist in nature?