Na+,K+-ATPase (NKA) is a membrane protein which assists in maintaining the electrochemical potential across the cell membrane. It has been suggested that the oligomerization of NKA may play a role in intracellular regulation of NKA activity. Monte Carlo simulations of NKA on a picket-fence membrane model were performed to examine if clustering has an effect on NKA efficiency. The results show that for a simple model of NKA interaction, oligomerization may drastically reduce the efficiency as measured in ATP turnover rate. Introducing a rate limit shows a clear separation between monomers and higher levels of oligomerization.
| Identifer | oai:union.ndltd.org:UPSALLA1/oai:DiVA.org:kth-308487 |
| Date | January 2022 |
| Creators | Jönsson, Jakob |
| Publisher | KTH, Tillämpad fysik |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Student thesis, info:eu-repo/semantics/bachelorThesis, text |
| Format | application/pdf |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | TRITA-SCI-GRU ; 2021:363 |
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