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- W3146064272 abstract "hydrolysis and Ca2þ transport is not well understood. Using solid-state nuclear magnetic resonance spectroscopy and functional assays, we investigated the differences in the interaction of phosphorylated SLN with SERCA compared to non-phosphorylated SLN with SERCA. Previous work in our lab demonstrates that the topology of SLN in complex with SERCA changes depending on SERCA’s conformation. As such, continuing work involves mapping the structural changes of phosphorylated SLN with the various conformations of SERCA. Overall, gaining a better understanding of how SERCA is regulated will add in the development of therapies for diseases resulting from improper calcium cycling." @default.
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- W3146064272 date "2015-01-01" @default.
- W3146064272 modified "2023-10-18" @default.
- W3146064272 title "Functional Analysis of Proton-Transporter at Single Molecule Level" @default.
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