Abstract—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.

Index Terms—Circular dichroism, muscle fatty acid Binding protein, locusta migratoria, self-association.

Abdul Hai and Nadeem A. Kizilbash are with the Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar, Saudi Arabia (e-mail: synavia@gmail.com, fsd707@ gmail.com).
Syeda Huma H. Zaidi is with the Department of Chemistry, Faculty of Science, Northern Border University, Arar, Saudi Arabia (e-mail: humazaidi@gmail.com).
Jamal Alruwaili is with the Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar, Saudi Arabia (e-mail: malkh1195@hotmail.com).

Cite: Abdul Hai, Nadeem A. Kizilbash, Syeda Huma H. Zaidi, and Jamal Alruwaili, "Indirect Evidence for Self Association of Muscle Fatty Acid Binding Protein from Locusta migratoria," International Journal of Bioscience, Biochemistry and Bioinformatics vol. 4, no. 5, pp. 419-422, 2014.