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On the basis of data from nuclear magnetic resonance spectroscopy, Dalibor Stys has built this model of the three-dimensional structure of the N-terminal domain of the phosphorylated form of the chloroplast light-harvesting complex. The phosphate group (phosphorus is yellow; oxygen is red) makes contacts that cause the polypeptide to fold into a compact, helix-like structure. Such a structure is seen by Anders Nilsson, using infra-red and circular dicroism spectroscopy, in both the N-terminal domain and the whole protein - provided the phosphate group is present. The domain becomes disordered when the phosphate group is removed. The whole protein binds chlorophyll, which absorbs and converts light energy. We aim to resolve the change in protein structure that is the foundation of regulation of light-harvesting in photosynthesis, the source of energy for life on earth.