Abstract: In this paper the energies of six X-ray crystallographic conformations of insulin B-chain helix have been analysed preliminarily and the conversion processes appeared between those conformations have been simulated on the VAX/VMS 780 computer, which showed that the conformational energies of molecule 1 B-chain helix were less than that of molecule 2 in those three crystals of insulin and the sharp changes of the energies in the conformational conversion processes were mainly the contributions of the interactions between a few atoms. Our studies indicated semi-quantitatively that the mode of sequential conformational changes one amino acid residue by one could not be present in the processes mentioned above. Our studies also indicated that the program ECEPP/2 was not suitable to the peptide model with more amino acid residues for the purposes of adding the hydrogen atoms to the model theoretically.