Control over overall shape and size in de novo designed proteins.

ABSTRACT: We recently described general principles for designing ideal protein structures stabilized by completely consistent local and nonlocal interactions. The principles relate secondary structure patterns to tertiary packing motifs and enable design of different protein topologies. To achieve fine control over protein shape and size within a particular topology, we have extended the design rules by systematically analyzing the codependencies between the lengths and packing geometry of successive secondary structure elements and the backbone torsion angles of the loop linking them. We demonstrate the control afforded by the resulting extended rule set by designing a series of proteins with the same fold but considerable variation in secondary structure length, loop geometry, β-strand registry, a

SUBMITTER: Lin YR 

PROVIDER: S-EPMC4603489 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature