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FEBS Lett. 1996 Oct 14;395(1):89-94.

Nereis sarcoplasmic Ca2+-binding protein has a highly unstructured apo state which is switched to the native state upon binding of the first Ca2+ ion.

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Institut National de la Santé et de la Recherche Médicale, Institut Curie, Orsay, France.


NSCP, a sarcoplasmic Ca2+/Mg2+-binding protein from Nereis diversicolor, shows an allosteric change during Ca2+ binding and a high positive cooperativity for Mg2+ binding. Here we report the results of CD and NMR experiments aiming to characterize the apo state and the Ca2+-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 Ca2+ determines large spectral changes bringing the molecule in a conformation which is very close to the native three Ca2+ state. Addition of the second and third Ca2+ shifts this equilibrium progressively towards the liganded conformation but affects only minimally the spectrum of the liganded species.

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