Abstract
NSCP, a sarcoplasmic Ca 2+/Mg 2+-binding protein from Nereis diversicolor, shows an allosteric change during Ca 2+ binding and a high positive cooperativity for Mg 2+ binding. Here we report the results of CD and NMR experiments aiming to characterize the apo state and the Ca 2+-induced conformational changes in this protein. Circular dichroism spectra of the apo form are indicative of a reduced helical structure. In contrast, NMR spectra show no element of regular secondary or tertiary structure. Addition of one Ca 2+ determines large spectral changes bringing the molecule in a conformation which is very close to the native three Ca 2+ state. Addition of the second and third Ca 2+ shifts this equilibrium progressively towards the liganded conformation but affects only minimally the spectrum of the liganded species.
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