The assembly of the bacterial ribosomal small subunit (SSU) begins with the folding of the five-way junction upon interaction with the primary binding protein S4. This complex contains the largest contiguous molecular signature, which is a conserved feature in all bacterial 16S rRNAs. In a previous study, we used all-atom molecular dynamics simulations to demonstrate that the coevolving signature in the N-terminus of S4 is intrinsically disordered and capable of accelerating the binding process through a fly-casting mechanism. In this paper, we capture the simultaneous folding and binding of the five-way junction and r-protein S4, by use of a structure-based Gō-potential implemented within the framework of the all-atom molecular dynamics CHARMM force field. Comparisons between the all-atom MD simulations and FRET experiments identify multiple metastable conformations of the naked five-way junction without the presence of S4. Using the hybrid MD-Gō simulations, different folding pathways are observed for the refolding of the five-way junction upon partial binding of S4. Our simulations illustrate the complex nature of RNA folding in the presence of a protein binding partner and provide insight into the role of population shift and the induced fit mechanisms in the protein:RNA folding and binding process.