Electrostatic force-driven conformational change in fatty acid-binding proteinsFatty acid-binding proteins (FABPs) are a class of cytoplasmic proteins that bind to long chain fatty acids. Their major role is to transport free fatty acids to the appropriate organelles for different metabolic fates within the cell. FABP is important for fatty acid trafficking due to the low solubility of fatty acids, a common characteristic of long-chain hydrocarbon molecules. To overcome this obstacle, fatty acids bind to FABP to improve their aqueous solubility and facilitate intracellular lipid transport. Fatty acids have been found to enter the nucleus and regulate gene transcription through interaction with nuclear receptor protein. The fatty acid serves as a signaling molecule for peroxisome proliferator-activated receptors (PPARs), which are a group of nuclear receptor proteins capable of mediating gene transcription. Previous research has shown that the FABP:FA complex transported into the cytosol translocates into the nucleus and interacts with PPAR. The FABP:FA complex releases bound FA from its B-barrel binding pocket upon binding with PPAR in the nucleus. Binding of FA with PPAR initiates gene expression leading to inhibition of chronic inflammation, as shown in numerous clinical studies using mammalian models. Despite functional discoveries about the FABP:FA complex, little is known about the biophysical forces behind the dynamics of ligand binding and release in FABP. The structure of FABP can be compared to that of lipocalin, which is a closely related structural homolog of FABP. Structural and conformational changes were detected in lipocalin upon association with ligand binding and release. Like the lipo structure counterpart...... middle of paper ......Ka value. Nucleic Acids Res. [online] http://nar.oxfordjournals.org/content/34/suppl_2/W48.short (accessed March 31, 2014).9. Koppole, S. (2003) An introduction to continuum electrostatics. , 1-1410. Georgescu, R., Alexov, E. and Gunner, M. (2002) Combining conformational flexibility and continuum electrostatics to calculate pK as in proteins. Biophysics. J. [online] http://www.sciencedirect.com/science/article/pii/S0006349502739404 (accessed March 31, 2014).11. Wu, H., Su, K., Guan, structural. Biochemistry. Biophysics. Acta… [online] http://www.sciencedirect.com/science/article/pii/S0005273609003769 (accessed March 31, 2014).12. Mcce, MCE GUNNER LAB – THE CITY COLLEGE OF NEW YORK GUNNER LAB – THE CITY COLLEGE OF NEW YORK,