The design protocol did not take functional/structural constraints into consideration. The designed sequences were sequentially compatible with the parent fold space. Expectedly their conformity with the parent structural fold could not be assumed and was hence determined through fold-recognition methods.
Three well represented structural folds were identified for this purpose. All the sequences used in the study were found to recognise the parent fold.
The ubiquitin-like designed sequences were used as a case study to identify the retention of function and structural attributes of the parent families. The physicochemical properties of the designed sequences were examined and compared with the parent families. The residue conservation was found to be intermediate to the parent protein families.