A current view of the mammalian aquaglyceroporins

Aleksandra Rojek1, Jeppe Praetorius, Jørgen Frøkiaer

  • 1Water and Salt Research Center, Institute of Anatomy, University of Aarhus, Aarhus C, Denmark.

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ATP Driven Pumps III: V-type Pumps

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Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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ATP Driven Pumps II: P-type Pumps

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Structure of Porins

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