Abstract
Fatty acid-binding proteins (FABPs) are a family of proteins that modulate the transfer of various fatty acids in the cytosol and constitute a significant portion in many energy-consuming cells. The ligand binding properties and specific functions of a particular type of FABP seem to be diverse and depend on the respective binding cavity as well as the cell type from which this protein is derived. Previously, a novel FABP (lcFABP; lc: Luciola cerata) was identified in the light organ of Taiwanese fireflies. The lcFABP was proved to possess fatty acids binding capabilities, especially for fatty acids of length C 14 –C 18 . However, the structural details are unknown, and the structure–function relationship has remained to be further investigated. In this study, we finished the 1 H, 15 N and 13 C chemical shift assignments of 15 N/ 13 C-enriched lcFABP by solution NMR spectroscopy. In addition, the secondary structure distribution was revealed based on the backbone N, H, C α , H α , C and side chain C β assignments. These results can provide the basis for further structural exploration of lcFABP.