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In all living organisms, the structure-function relationship of proteins has been widely studied. In the late 1990s, proteins which, in their native state, were poorly structured were called IDPs for "intrinsically disordered proteins". They can be fully or partially disordered. The presence of disorder within these proteins gives them a high flexibility or plasticity, sometimes allowing them to perform several functions. I will present results obtained on CP12, a chloroplastic protein that belongs to the IDP family and that is a jack-of-all trade and a master of the Benson-Bassham Calvin cycle.