Protein conformational transitions in sarcoplasmic reticulum membranes

Fourier-transform infrared spectroscopic studies of sarcoplasmic reticulum proteins, in H2O and D2O, suggest that 10 mM ATP induces a conformational change in those proteins, increasing their contents in alpha-helical and beta-antiparallel structures. Ca2+ on the contrary, is seen to reduce the proportion of alpha-helix and increase the contribution of random coil.