Carotenoids are ancient pigment molecules that, when associated with proteins, have a tremendous range of functional properties. Unlike most protein prosthetic groups, there are no recognizable primary structure motifs that predict carotenoid binding, hence the structural details of their amino acid interactions in proteins must be worked out empirically. Here we describe our recent efforts to combine complementary biophysical methods to elucidate the precise details of protein-carotenoid interactions in the Orange Carotenoid Protein and its evolutionary antecedents, the Helical Carotenoid Proteins (HCPs), CTD-like carotenoid proteins (CCPs).
Keywords: CTD-like carotenoid proteins (CCP); Carotenoid; Chromophore; Helical carotenoid protein (HCP); Hydrogen-deuterium exchange (HDX); Orange carotenoid protein (OCP); Photoprotection; Protein crystallography; Small angle X-ray scattering (SAXS); X-ray footprinting mass spectrometry (XFMS).
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