A number of organisms have been found to be capable of surviving severe water deficit as a result of extreme drought and cold in nature by entering a state of suspended animation (i.e., anhydrobiosis or life without water) [1]. Although the precise molecular repertoire of desiccation tolerance in anhydrobiotic organisms is still not fully understood, results from recent studies indicate the crucial role of stress proteins such as the late embryogenesis abundant (LEA) proteins [2]. LEA proteins have been proposed to play a variety of roles in protecting biologicals from damaging by dehydration stress such as molecular chaperone and shield, ion chelator, antioxidant, and space filler. The multifunctional capacity of LEA proteins has been attributed in part to their structural plasticity: they are unfolded and when fully hydrated and become folded during water deficit [1]. However, the structural stability of LEA protein in response to desiccation is still not fully understood. In this study, the structure alteration of a group 3 LEA protein from an anhydrobiotic nematode (AavLEA1) [2] were investigated using the molecular dynamics (MD) simulation approach to understand the structural stability at different water contents.

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