The role of intrinsically disordered proteins under conditions of abiotic stress
The ability of extremophile organisms to survive hostile conditions has caused us to reassess the requirements for life. Scientists and engineers strive to elucidate extremophile survival mechanisms that might allow the development of new technologies for preserving biological materials. LEA proteins are linked to the acquisition of cold and desiccation tolerance in plants and animals. As intrinsically disordered proteins, LEA proteins are inherently tolerant to stress-induced denaturation, and LEA proteins have been shown to protect globular proteins, such as pig citrate synthase and rabbit lactate dehydrogenase, and a human cell proteome from abiotic stresses. Our current results do not appear to align with the conventional models of interactions and, has led us to propose an additional protection mechanism: the preferential adsorption of LEA proteins at air/water interfaces, where the globular proteins are shielded from the irreversible damage at the interface. The aim of this proposal is to use neutron reflection to assess our new hypothesis by studying study the competitive adsorption an LEA protein at the air/water interface.
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ROUTH Alexander; BARKER Robert; HOUGH Andrea; TUNNACLIFFE Alan; WATSON Matthew and YUEN Fanny. (2014). The role of intrinsically disordered proteins under conditions of abiotic stress. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-540
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