About the Project
In this project, this technique will be applied to investigate the conformational changes of individual enzyme molecules during catalytic turnover. Simulations will provide the essential atomic‐level analysis to interpret single‐molecule measurements to reveal the dynamics of enzyme catalysis and thermoadaptation. The project will also investigate how enzymes are adapted to work at different temperatures. Enzymes have an optimum temperature at which they are most catalytically active. Above that temperature, they become less active. The textbook explanation that enzymes unfold at higher temperatures does not explain this, most obviously for cold‐ adapted enzymes which are stable and folded, but less active, above their optimum temperature. In contrast to simple ‘chemical’ catalysts, they become less active at higher temperatures even though they maintain their functional shape. Instead, a basic physical property ‐ the heat capacity ‐ explains and predicts the temperature dependence of enzymes. The heat capacity changes during the reaction and is ’tuned’ by the enzyme’s dynamics to give the optimal temperature. The theory that describes this ‐ macromolecular rate theory, (MMRT) ‐ applies to all enzymes, and so has a critical role in predicting metabolic activity as a function of temperature. Experiments are revealing characteristics of MMRT at the level of cells, whole organisms and even ecosystems. This means that it is important in understanding the response of biological systems to temperature changes, for example, how ecosystems will respond to climate change.
This project will use simulations and experiments to reveal how enzyme dynamics are tuned to determine optimum temperatures of catalysis. It will analyse and predict effects of mutations and identify novel principles of enzyme engineering.
Apply here: https://www.swbio.ac.uk/advancing-the-frontiers-of-bioscience-discovery/
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