Examples of Designed Proteins
The early 21st century saw the creation of small proteins with real biological functions including chiroselective catalysis, ion detection, and antiviral behaviour. Using computational methods, a protein with a novel fold (Top7) was designed in 2003, as well as sensors for unnatural molecules. Recent computational redesign was capable of experimentally switching the cofactor specificity of Candida boidinii xylose reductase from NADPH to NADH.
Five more protein structures were designed, synthesized, and verified in 2012. These new proteins serve no biological function, but the structures are intended to act as building blocks that can be expanded to incorporate functional active sites. The structures were found computationally by using new heuristics based on analyzing the connecting loops between parts of the sequence that specify secondary structures.
On the other hand, it is widely believed that not all possible protein structures are designable, which means that there are compact configurations of the chain which no sequences can fold to. In particular, conformations which are poor in secondary structures are unlikely to be designable. The designability of given structures is still poorly understood.
Read more about this topic: Protein Design
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