PROTACs are heterobifunctional molecules in which a linker joins a ligand binding to a protein of interest (POI), conferring specificity, and an E3 ubiquitin ligase. The formation of the ternary complex leads to subsequent ubiquitination, achieving POI degradation and thus, targeted knockdown. While the unique mechanism of action provides promising therapeutic applicability beyond traditional small molecules, PROTACs design is challenging. PROTACs are comparably large molecules, typically existing beyond 'Lipinski's rules' and thereby posing a design challenge since experience is limited. Moreover, linker design is challenging due to the relatively high conformational flexibility present in longer linkers and has mostly deferred to empirical structure-activity relationship (SAR) studies, often necessitating numerous iterations of design-make-test-analyze (DMTA) cycles. Therefore, there is a need for improved linker design to improve overall PROTACs design.