Studies of Molecular Energy Changes in AQP5 in the Presence and Absence of Water Using Computational Method
Trends in Peptide and Protein Sciences,
Vol. 4 (2019),
1 January 2019
,
Page 1-7 (e4)
https://doi.org/10.22037/tpps.v4i0.23908
Abstract
Aquaporins (AQPs) are water channel proteins. Up to now, 13 AQPs have been known in mammals. AQPs play a key role in water osmotic flow in various cells. the members of aquaporin protein family have been identified as H2O transposters across organelle and plasma membranes. AQPs of the aquaammoniaporin type are highly permeable for water and ammonia. In this study, we have evaluated the structure of AQP5 using two computational methods. We investigated the potential and kinetic energy, as well as maximum and minimum difference of atomic charge for AQP5. The atomic study of AQP5 protein showed that the minimum and maximum value of atomic charge in the presence and absence of water were related to sections (1-15). The water effect is generally considered to be the major driving force in the folding of AQP5. different sections of AQP5 behaved different in the presence or absence of water, and have different functionalities. Also, the absolute value of atomic charge difference for AQP5 sections was proven as an important feature in protein structural changes.
HIGHLIGHTS
•AQP5’s function and structure are dependent on the presence and absence of water.
•The presence of water molecules around AQP5 protein causes changes in dynamic properties.
•The optimum functions of AQP5 are arisen at low energy levels and the presence of water.
•kinetic energy for AQP5 protein in mode of no water has the lowest fluctuations but in presence of water considerable fluctuations are seen.
- Aquaporins
- Computational simulation
- Energy
- Membrane Channel
- Water.
How to Cite
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