In silico modelling of wild-type, pIII N-terminal 30-amino-acid fragment and several peptides fused at that site showed a probable secondary structure of the peptide and terminal region of pIII (Fig. ) . The native helical fragment at N-terminus was quite affected for analysed A3, C9 and D11 clones. Nevertheless, undisturbed amplification and titration of these clones exclude the significant impact of additional fragments on bacteria recognition and infection, consistent with literature reports . N-terminus of cardiac TnT is a long, helical structure exposing polar residues outside the helix, according to in silico simulation of appropriate sequence in PEP-FOLD3 . Structures were generated using .