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Fatty acids (FA) play an important role in biological functions, such as membrane homeostasis, metabolism, and as signaling molecules. FadL is the only known protein that uptakes long-chain fatty acids in Gram-negative bacteria, and this uptake has traditionally been thought to be limited to fatty acids up to 18 carbon atoms in length. Recently however, it was found <i>Vibrio cholerae</i> has the ability to uptake fatty acids greater than 18 carbon atoms and this uptake corresponds to bacterial survivability. Using <i>E. coli’s</i> FadL as a template, <i>V. cholerae</i> FadL homologs <i>vc1042</i>, <i>vc1043</i>, and <i>vca0862</i> have been computationally folded, simulated on an atomistic level using Molecular Dynamics, and docked <i>in silico</i> to analyze the FadL transport channels. For the <i>vc1042</i> and <i>vc1043</i> homologs, these transport channels have more structural accommodations for the many rigid unsaturated bonds of long-chain polyunsaturated fatty acids, while the <i>vca0862</i> homolog was found to lack transport channels within the signature beta barrel of FadL proteins.