Small β-hairpin peptides as well as three-stranded WW domains have been used as models for the folding of β-hairpins in larger proteins. Previous studies of the FBP28 WW domain proposed that side chain contacts between residues in the strands and not the precise order of backbone hydrogen bond formation guide β-hairpin folding. But how applicable is the folding of model systems, such as FBP28 WW domain, to the folding of β-structure in larger proteins with conventional hydrophobic cores? Here we present multiple unfolding molecular dynamics simulations of three proteins that share a double hairpin motif structurally similar to WW domains: cold shock protein A (CspA), cold shock protein B (CspB) and glucose permease IIA domain. The motif forms a sheet in both cold shock proteins while the double hairpin is part of a larger, 7-stranded β-sheet in the IIA domain. We characterized the unfolding pathways of each protein, all showing no consistent order to the loss of backbone hydrogen bonds, similar to the FPB28 WW domain. The smaller cold shock proteins both lose contacts between the β-hairpins and the hydrophobic core early in the unfolding simulations, while the larger, more complex IIA domain maintains contacts to the core and surrounding β-strands later in the simulations, resulting in a more varied unfolding pathway. We show that the larger protein context affects the details of the unfolding pathway of the double hairpin motif.