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Extreme biophysics: single molecule characterisation of extremophilic protein folding

Mid-Term Report Summary 2 - EXTREME BIOPHYSICS (Extreme biophysics: single molecule characterisation of extremophilic protein folding)

Life has adapted to a vast range of environmental conditions and it is now difficult to find any place on Earth devoid of life. Some conditions are extreme in the sense of being unfavourable to most eukaryotic life forms. The adaption of proteins played a key role in enabling extremophilic organisms to colonise such ecological niches. Understanding the physical properties of proteins from extremophilic organisms and their remarkable preservation capability is not only of fundamental interest, but also pivotal to our ability to rationally engineer biological materials for exploitation.

We are developing quantitative biophysical approaches to characterise the physical mechanisms of protein folding and stability in extreme environments. We use a force spectroscopy instrument to examine the conformational dynamics of single extremophilic proteins. This technique is used to apply a stretching force along the end-to-end length of the protein, driving proteins to a fully extended unfolded state. By examining single molecules one at a time, the individual dynamics of protein subpopulations can be measured, revealing information which may be crucial for designing ‘artificial’ extremophilic proteins.

A single molecule approach provides a new perspective and reveals novel insight into the mechanisms of protein folding. By exploring the structural limitations of extremophilic proteins we aim to uncover universal rules determining how proteins fold. Such knowledge will be invaluable for the de novo design of proteins with desired properties. This work will reveal critical information on the physics and function of proteins and provide the foundations for developing biologically inspired materials.