Molecular distance measurements reveal an (alpha beta)(2) dimeric structure of Na+/K+-ATPase - High affinity ATP binding site and K+-activated phosphatase reside on different alpha-subunits

Abstrakt

Forster energy transfer was used to measure the distance between high (E(1)ATP) and low (E(2)ATP) substrate binding sites of Na+/K+-ATPase.

Klíčová slova

• Tomáš Obšil
• 221951311 Na+
• K+-ATPase
• fluorescence
• energy-transfer
• ATP binding site