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.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D005583:Fourier Analysis; D008565:Membrane Proteins / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013055:Spectrophotometry, Infrared
D008565:Membrane Proteins; D000255:Adenosine Triphosphate; D002118:Calcium