Abstract
This chapter reviews the molecular biology, biochemical, and NMR methods that we used to study the structural dynamics, membrane topology, and interaction of phospholamban (PLN), a small regulatory membrane protein involved in the regulation of the sarcoplasmic reticulum Ca-ATPase (SERCA). In particular, we show the progression of our research from the initial hypotheses toward understanding the molecular mechanisms of SERCA’s regulation, including the effects of PLN oligomerization and posttranslational phosphorylation. Finally, we show how the knowledge of the molecular mechanism of the structural dynamics and topology of free and bound proteins can lead to the rational design of PLN analogs for possible use in gene therapy.
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Acknowledgment
This work was supported by grants to GV from the National Institutes of Health (GM64742, HL80081, GM072701) and NJT (AHA 0515491Z). PISEMA spectra were acquired at the NHMFL, Tallahassee, FL (DMR-0084173). NMR instrumentation at the University of Minnesota High Field NMR Center was funded by the National Science Foundation (BIR-961477) and the University of Minnesota Medical School.
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Veglia, G., Ha, K.N., Shi, L., Verardi, R., Traaseth, N.J. (2010). What Can We Learn from a Small Regulatory Membrane Protein?. In: Lacapère, JJ. (eds) Membrane Protein Structure Determination. Methods in Molecular Biology, vol 654. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-762-4_16
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DOI: https://doi.org/10.1007/978-1-60761-762-4_16
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