Abstract

Using the verified theory of absolute reaction or transition state theory to calculate the temperature-dependent viscosity tuned by aquaporins (which are membrane proteins) we can capture the glass transition states considering the onset viscosity and their role in vitrification and dehydration for surviving the anabiotic states (e.g., larvae of the cryptobiotic sleeping chironomid (P. vanderplanki) accumulate glassy trehalose under desiccation conditions). We will demonstrate the viscosity-dominated transport control considering aquaporins' role in water removal during the onset of dehydration-induced periods via the selected activation energy as well as the activation volume with the presumed wavy-roughness along the sub-nano domains. Our calculations showed that the activation-volume effect is more dominated than the activation-energy effect considering the induced increase of viscosity. Our low-temperature results imply that the trapping of conformational substates at low temperature may result more from energy barriers internal to the protein than from high solvent viscosity.

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