The figure below is an excerpt taken from a paper titled “Ch…
The figure below is an excerpt taken from a paper titled “Chain Length-dependent Binding of Fatty Acid Anions to Human Serum Albumin Studied by Site-directed Mutagenesis”, published in 2006 in the Journal of Molecular Biology. Human serum albumin (HSA) is the most abundant plasma protein and a versatile carrier that transports a wide range of ligands. It binds long‑chain fatty acids at multiple high‑affinity sites located across distinct protein subdomains, using hydrophobic pockets and specific hydrogen‑bond/ionic interactions to stabilize the anionic carboxylate headgroups. By buffering and distributing fatty acids between tissues, HSA modulates their bioavailability, prevents micelle formation and toxicity in plasma, and delivers them to cells via reversible, concentration‑dependent binding. The graphs presented in Figure 1 compare the binding of 4 different fatty acids of varying length (octanoate = 8 carbons, decanoate = 10 carbons, laurate = 12 carbons, myristate = 14 carbons in length) to the wildtype HSA and to a mutant HSA they created in the lab (denoted as R410A, which indicates that the amino acid at position 410 in the wildtype protein is normally an R but the researchers intentionally changed it to an A). Finish the following sentence: “Based upon the plots, the fatty acids bind ____ to the recombinant mutant HSA than they bind to the wildtype HSA”