We are creating folded polyprotein hydrogels which possess specific biological function capabilities, enabling dynamic changes in mechanical and structural properties in response to biomolecular cues. This is achieved through a cross length scale, physics-based approach which will translate knowledge of the nanoscale biophysics of folded proteins to the mesoscale architecture and function of novel folded polyprotein hydrogels. By understanding the physics of the building block (the folded protein) and its connectivity (the polyprotein network) we are creating a platform for the production of nove, biomaterials.
Life in extreme environments
Extremophiles are organisms which survive and thrive in extreme environments. The proteins from extremophilic single-celled organisms are structurally stable and functionally active under extreme physical and chemical conditions. We are using single molecule force spectroscopy to mechanically manipulate proteins from extremophilic organisms to gain information about their stability, flexibility and underlying energy landscapes.
Single molecule manipulation
One of the most exciting developments in the field of biological physics in recent years is the ability to manipulate single molecules and probe their properties and function. Single molecule force spectroscopy has become a powerful tool to explore the response of biological molecules, including proteins, DNA, RNA and their complexes, to the application of an applied force. The force versus extension response of molecules can provide valuable insight into its mechanical stability, as well as details of the underlying energy landscape.
Physics of Cryopreservation
Cryoprotectant molecules are widely used in basic molecular research through to industrial and biomedical applications. The molecular mechanisms by which cryoprotectants stabilise and protect molecules and cells, along with suppressing the formation of ice, are incompletely understood. To gain greater insight, we complete experiments to determine the structure of cryoprotectant solutions at low temperatures. Our investigations combine neutron diffraction experiments with isotopic substitution and computational modelling to determine the atomistic level structure of the mixtures. We examine the local structure of the system including the water structure.
Recent studies suggest that hydrophilic interactions play an important role in controlling self-assembly in biological processes. To explore the effect of temperature on this interaction we use neutron diffraction coupled with isotopic substitution and computational modelling to examine the structure of biological molecules in solution. These studies are important because they highlight the necessity to consider hydrophilic interactions in the self-assembly and association of biological systems, and not just the more traditional hydrophobic interaction.
Polypeptide chain aggregation
- Structure and hydration of amino acids in aqueous solution
- Structural examination of polypeptide chains
- Biophysical characterisation of polypeptide chain stabilty
- Kinetics of aggregation of polypeptide chains