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They were able to compare the resistance or stability of all the titins being studied.
"In this study, we realised that the mechanochemical stability of the proteins depended on the number of disulphide bridges displayed by the titin, which are sulphur-sulphur bonds between two cysteine residues." They were able to see that the ancestral proteins were more resistant than those of today's animals, and they had more disulfide bridges than the modern ones.
"The complete genome of many animals was already available, so the first thing we did was to build a phylogenetic tree with the titin sequences of around thirty tetrapods.