Fatty acid binding proteins are involved in the storage and transport of long chain fatty acids. This study about the muscle fatty acid binding protein of Locusta migratoria (LM-FABP) was pursued by the use of far-UV Circular Dichroism (CD) spectroscopy. It provides indirect evidence that the protein self-associates in solution. A hydrophobic patch on the surface of LM-FABP, reported earlier, can mediate self-association between the protein monomers. The property of self-association can also affect the activity of membrane-bound enzymes in locusts such as Adenine Nucleotide Translocase (also known as the ADP/ATP translocator) which is fatty acid or acyl coenzymeA dependent. proteins. The self-association or aggregation of proteins results in the development of such diseases as Down's syndrome, Alzheimer's disease (7), cataracts (8), (9) and many others. The formation of inclusion bodies is a major problem in the overexpression of recombinant proteins (10)-(13), while the production and in vivo delivery of protein drugs is often complicated by association (14). Adenine Nucleotide Translocase (ANT) is an integral protein of the inner mitochondrial membrane that plays an important role in cellular bioenergetics (15), apoptosis (16) and cell signaling (17). ANT catalyzes the exchange of ADP for ATP across the inner mitochondrial membrane thereby coupling oxidative phosphorylation to cell metabolism. The property of self-association of muscle FABP of Locusta migratoria was investigated by Circular Dichroism (CD) spectroscopy. Self-association of LM-FABP can produce an effect on the activity of membrane-bound enzymes in insects such as Adenine Nucleotide Translocase (also known as the ADP/ATP translocator) which is fatty acid or acyl coenzymeA dependent.