Aquaporins are membrane water channels that play critical roles in controlling the water contents of cells. These channels are widely distributed in all kingdoms of life, including bacteria, plants, and mammals. More than ten different aquaporins have been found in human body, and several diseases, such as congenital cataracts and nephrogenic diabetes insipidus, are connected to the impaired function of these channels. They form tetramers in the cell membrane, and facilitate the transport of water and, in some cases, other small solutes across the membrane. However, the water pores are completely impermeable to charged species, such as protons, a remarkable property that is critical for the conservation of membrane's electrochemical potential, but paradoxical at the same time, since protons can usually be transferred readily through water molecules. The present investigation is profound manifesting of thermodynamics characteristics of the impressive AQP4 role in biology. To clarify the majestic AQP4 role in biology, it was modeled. So we use pc-based modeling and simulation software package called HyperChem by applying four different force fields. The results of our simulations have now provided new insight into the optimal stability of AQP4.
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