Synthetic beta-solenoid proteins with the fragment-free computational design of a beta-hairpin extension.

ABSTRACT: The ability to design and construct structures with atomic level precision is one of the key goals of nanotechnology. Proteins offer an attractive target for atomic design because they can be synthesized chemically or biologically and can self-assemble. However, the generalized protein folding and design problem is unsolved. One approach to simplifying the problem is to use a repetitive protein as a scaffold. Repeat proteins are intrinsically modular, and their folding and structures are better understood than large globular domains. Here, we have developed a class of synthetic repeat proteins based on the pentapeptide repeat family of beta-solenoid proteins. We have constructed length variants of the basic scaffold and computationally designed de novo loops projecting from the scaffold co

SUBMITTER: MacDonald JT 

PROVIDER: S-EPMC5027453 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature