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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Positive functional synergy of structurally integrated artificial protein dimers assembled by Click chemistry Harley L. Worthy , Husam Sabah Auhim , W. David Jamieson , Jacob R. Pope , Aaron Wall , Robert Batchelor , Rachel L. Johnson , Daniel W. Watkins , Pierre Rizkallah , Oliver K. Castell , D. Dafydd Jones Communications Chemistry 2 DOI: 10.1038/s42004-019-0185-5 Diamond Proposal Number(s): [14843] Open Access Show Abstract ▼ Abstract: Construction of artificial higher order protein complexes allows sampling of structural architectures and functional features not accessible by classical monomeric proteins. Here, we combine in silico modelling with expanded genetic code facilitated strain promoted azide-alkyne cycloaddition to construct artificial complexes that are structurally integrated protein dimers and demonstrate functional synergy. Using fluorescent proteins sfGFP and Venus as models, homodimers and heterodimers are constructed that switched ON once assembled and display enhanced spectral properties. Symmetrical crosslinks are found to be important for functional enhancement. The determined molecular structure of one artificial dimer shows that a new long-range polar network comprised mostly of organised water molecules links the two chromophores leading to activation and functional enhancement. Single molecule analysis reveals the dimer is more resistant to photobleaching spending longer times in the ON state. Thus, genetically encoded bioorthogonal chemistry can be used to generate truly integrated artificial protein complexes that enhance function.	Jul 2019

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I03-Macromolecular Crystallography
I04-Macromolecular Crystallography

Positive functional synergy of structurally integrated artificial protein dimers assembled by Click chemistry