Abstract

Adipocyte fatty acid binding protein-4 (FABP4) is a 132-aa intracellular lipid binding protein involved in the transport of fatty acids between cell membranes and organelles. FABP4 participates in several pathways including lipolysis and lipogenesis, and is involved in lipid and energy metabolism related diseases such as diabetes. Although the x-ray structure of FABP4 has been determined and binding to several of its hydrophobic ligands well characterized, the transitions in the structural dynamics upon ligand binding has yet to be determined. Here, solution NMR experiments will be carried out on 15N and 13C labeled FABP4 to study the structural transitions between its free and bound states. Spin relaxation measurements will also be used to reveal any changes that occur upon binding of FABP4 to its hydrophobic ligands.

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