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Binding of uniformly 13 C labelled ATP to Na,K-ATPase was studied by 13 C cross-polarization magic-angle spinning (CP-MAS) NMR. In the presence of 30mM Na + , and with sample- and time-averaging, NMR spectra obtained at 4°C exhibited several resonances for the bound nucleotide. Chemical shifts suggested that site-specific changes in the micro-environment or conformation of...
The structure of a synthetic peptide corresponding to the fifth membrane-spanning segment (M5) in Na + ,K + -ATPase in sodium dodecyl sulfate (SDS) micelles was determined using liquid-state nuclear magnetic resonance (NMR) spectroscopy. The spectra reveal that this peptide is substantially less α-helical than the corresponding M5 peptide of Ca 2+ -ATPase. A well-defined α-helix...
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