Life in extreme environments: The role of intrinsically disordered proteins at ice-liquid water interfaces
The ability of extremophile organisms to survive hostile conditions has intrigued scientists as they develop new technologies to preserve biological materials. Intrinsically disordered proteins (IDPs), such as LEA proteins, have been found to be upregulated in some plants and animals as these organisms gain cold and desiccation tolerance. LEA proteins have been shown to protect globular proteins, such as pig citrate synthase (CS) and rabbit lactate dehydrogenase, and a human cell proteome, from abiotic stress. The mechanism behind these protective abilities is still unclear, but leading hypotheses involve chaperone or shield interactions. However, our preliminary experiments suggest that these interactions are insufficient to explain the protection observed. This has led us to propose that LEA proteins preferentially adsorb onto surfaces generated in the freeze-thaw process, thereby excluding folded proteins from interfaces where they would undergo irreversible aggregation. The aim of this study is to investigate the adsorption and structural conformation of an LEA protein and CS at an ice/water interface analogue in order to better understand how IDPs protect globular proteins.
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ROUTH Alexander; BARKER Robert; TUNNACLIFFE Alan; WATSON Matthew and YUEN Fanny. (2015). Life in extreme environments: The role of intrinsically disordered proteins at ice-liquid water interfaces. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-710
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