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Assembling a Molecular Switch: Using Protein Folding Mechanisms to Guide the Design of Novel Regulatory Elements

The quaternary‐structure of oligomeric proteins has far reaching implications. Namely, the ability to form dimeric or higher‐order oligomers dramatically enhances the biological activity of many proteins; this is of crucial importance for DNA‐binding proteins. From the vantage point of evolution, it may be simpler to create complex biological machinery from smaller protein subunits rather than from a massive single chain system. Likewise, understanding the relative stability and dynamic inter‐conversion during the protein folding process of oligomeric systems can provide insight into the energetics underlying biological regulatory mechanisms and assembly, in addition to the physicochemical properties that result in protein misfolding associated with disease. In turn, well‐defined folding‐assembly mechanisms can be used as a framework to create novel protein assemblies that are functional; this collection of engineered molecular switches can be used in a range of bio‐technological applications.