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The Cold Never Bothered Me Anyway Measuring the Forces at Work Defending Protein-DNA Interactions from Temperature Extremes. K. Ellen Kendrick*†, David J. Brockwell†, Lorna Dougan*† *Molecular and Nanoscale Physics Group, University of Leeds †Astbury Centre for Structural Molecular Biology, University of Leeds Extremophilic Proteins Psychrophile Optimum Temperature 10 °C Measuring Protein Mechanics The Mechanical properties of proteins can be measured using an Atomic Force Microscope. This uses the deflection of a small cantilever to measure piconewton forces and can be utilised to pull apart proteins one molecule at a time. The force required to unfold a protein indicates it’s stability, and this method can be used to measure other mechanical data. need flexibility to bind King George island, Antarctica Life has been found across the planet in conditions that vary greatly in temperature, acidity, salinity and aridity. Proteins are the molecules that do the work in keeping cells alive, so to survive in extreme conditions these proteins need to be adapted. These adaptations adjust the forces that hold the molecules together. The proteins are then able to carry out the processes essential to cell survival. This includes the fundamental mechanism of interactions between proteins and the nucleic acids, DNA and RNA. Mesophile Optimum Temperature 37 °C Performing this unfolding experiment in the presence and absence of single stranded DNA (ssDNA) we can explore the properties that allow it to function at specific temperatures. Flexibility is key for binding, and measurements so far have shown an increase in flexibility when ssDNA is bound to the mesophilic cold shock protein. Combining this with Nuclear Magnetic Resonance experiments, another way to measure flexibility, we plan to compare the DNA needs to constantly be copied, psychrophilic and mesophilic Cold Shock Protein for clues as to repaired and read for healthy growth and reproduction. Any mistakes have the how the psychrophilic protein functions at lower temperatures. Temperate Soils The Cold Shock Protein has been identified in many organisms from various environments. This protein binds to nucleic acids when there is a drop in temperature and is thought to help maintain protein production. It has a highly conserved structure but small differences in the amino acid sequence of extremophilic Cold Shock proteins change their flexibility, allowing them to move about and operate at the environment temperature of the organism. This is one of the reasons they have been chosen as model proteins to explore how these adaptations are encoded at the molecular level. Protein-DNA Interactions Cold temperatures can cause nucleic acids to fold into shapes that cannot be read. Applications potential to cause huge problems for the organism. Much of this work is carried out by proteins. Proteins as Building Blocks Protein based hydrogels are exciting new Protein based Hydrogel Structure materials being explored for biomedical and Cold Shock Proteins bind to nucleic acids to keep them from folding incorrectly. 1nm Understanding protein evolution Hyperthermophile Hydrothermal vents, e.g. Vulcano, Italy Optimum Temperature 80 °C biotechnological applications, with the potential for smart materials which 10mm respond to external stimuli. These hydrogels could be applied to wound healing, targeted drug delivery and have the advantage of being biocompatible. Mechanically and thermally stable proteins are required for this application. Understanding extremophiles helps us appreciate how life may have evolved in past climates. It also exposes the limits of what can be survived, which may aid the search for life outside our planet. Acknowledgements We are grateful to the White Rose University Consortium and European Research Council for funding and to the rest of the Dougan group for useful discussions and support.