The three-dimensional structure of aquaporin-1
Article Abstract:
The mercury-sensitive water channel aquaporin-1 (AQP1) has been identified as the specialized water pore in the plasma membrane of red blood cells. This is a homotetramer which contains four independent aqueous channels. It is possible to present a three-dimensional structure of AQP1 using cyro-electron microscopy. This approach allows the aqueous pore in the AQP1 molecule to be identified and shows how the tetrameric complex in the membrane is structured.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
Article Abstract:
Research using high-resolution electron crystallography shows that the transmembrane protein bacteriorhodopsin contains charged residues on either side of the membrane surface. The surface membrane contains almost 248 amino acids. Four glutamate residues are known to exist around the proton channel entrance the extracellular side of the membrane. Four aspartic acids are known to exist around on the cytoplasmic side of the membrane.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Structural determinants of water permeation through aquaporin-1
Article Abstract:
Research is presented concerning the development of an atomic model which provides a possible solution for the physiological behavior of membranes which are impermeable to protons but permeable to water.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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