Acyl carrier protein (ACP) plays a central role in fatty acid biosynthesis, acting as a molecular “shuttle” that carries, protects, and delivers elongating acyl chains to various enzymatic partners. However, the high flexibility of ACP and the instability of its thioester‐linked intermediates have long hindered detailed structural characterization of its dynamic behavior.
Researchers reveal acyl chain length-dependent conformational dynamics of acyl carrier protein
