From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles.

ABSTRACT: The design of completely synthetic proteins from first principles-de novo protein design-is challenging. This is because, despite recent advances in computational protein-structure prediction and design, we do not understand fully the sequence-to-structure relationships for protein folding, assembly, and stabilization. Antiparallel 4-helix bundles are amongst the most studied scaffolds for de novo protein design. We set out to re-examine this target, and to determine clear sequence-to-structure relationships, or design rules, for the structure. Our aim was to determine a common and robust sequence background for designing multiple de novo 4-helix bundles. In turn, this could be used in chemical and synthetic biology to direct protein-protein interactions and as scaffol

SUBMITTER: Naudin EA 

PROVIDER: S-EPMC9533478 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature