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In this study, the tandem PDZ1\u2013PDZ2 domains of the scaffold protein X11, a system of particular interest due to its previously reported asymmetric folding and unfolding behavior as well as its propensity to form transient misfolded intermediates, are investigated. Through extensive mutational work and in\u2010depth kinetic folding analysis, the folding behavior of this multidomain construct is dissected, and a comparative analysis with its isolated PDZ domains is also performed. The results reveal that folding and unfolding proceed through distinct pathways with PDZ2 folding rapidly and independently, while PDZ1 folds more slowly and only upon engagement of an autoinhibitory regulatory tail. Despite these differences, the folding mechanisms of each domain are conserved when studied in isolation, with deviations largely confined to functionally relevant and frustrated regions. 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