| Autor: |
Prêcheur B; Institut National de la Santé et de la Recherche Médicale, Institut Curie, Orsay, France., Cox JA, Petrova T, Mispelter J, Craescu CT |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1996 Oct 14; Vol. 395 (1), pp. 89-94. |
| DOI: |
10.1016/0014-5793(96)01007-1 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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