Mirror-image translation could then be achieved in vitro, using D-aminoacyl-tRNA synthetases to load the L-tRNAs along with the mirror-imaged translational factors. Subsequently, all Dproteins needed in mirror-image life, racemic protein crystallography and D-targets for mirror-image phage display may be obtained by suppling the exogenous L-nucleic acids encoding the desired protein. Perhaps, preparation of entire D-polypeptides can also be achieved using "Flexizyme" technology, which has been reported to incorporate D-amino acids into peptide chains without using enantiomeric translation components. Chemical synthesis remains superior at atomistic control allowing researchers to incorporate building blocks without constraints associated with ribosome-based systems. Complex D-protein targets can be achieved via: engineering of split enzymes, mutational installation of suitable ligation sites and in silico design of accessible D-enzymes. For protein crystallography, smaller D-proteins can be used to facilitate crystallization of complex L-proteins by quasi-racemic protein crystallography. In addition, discovery of D-peptide binders could be achieved via computational-based approaches. Together, while there are challenges remained to be solved, D-polypeptide research remains to have strong potentials that can generate explosive impacts on numerous research topics. Quenched by thiol catalyst. Native Cys must be protected.