Kurt D Torgersen

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We have used chemical synthesis, functional reconstitution, and electron paramagnetic resonance (EPR) to probe the functional dynamics of phospholamban (PLB), which regulates the Ca-ATPase (SERCA) in cardiac sarcoplasmic reticulum. The transmembrane domain of PLB inhibits SERCA at low [Ca(2+)], but the cytoplasmic domain relieves this inhibition upon Ser16(More)
Phospholamban (PLN) regulates calcium translocation within cardiac myocytes by shifting sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) affinity for calcium. Although the monomeric form of PLN (6 kDa) is the principal inhibitory species, recent evidence suggests that the PLN pentamer (30 kDa) also is able to bind SERCA. To date, several membrane(More)
  • Albert H Beth, Thomas, L R Dalton, J S Hyde, James, J E Mccaffrey +5 others
  • 2012
It has long been appreciated that the rotational diffusion coefficient (D r) and hence the rotational correlation time (t r) of a transmembrane protein about its membrane normal axis is predicted to be highly sensitive to its cylindrical radius (e.g., Saffman and Delbrück (1)). Due to the highly vis-cous nature of a cellular membrane or a membrane bilayer,(More)
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