The molecule hylambatin on its structured particularities and physiologic functions pertains to tachykinin neuropeptides. The molecule hylambatin on its structured particularities and physiologic functions pertains to tachykinin neuropeptides. The spatial structure and conformational properties of some fragments of hylambatin tachykinin peptide have been investigateby molecular mechanics method. It is khown that this molecule has different dipeptide segment L-Met-L-Met at the C-terminus in change from tachykinins. As results of given investigation were determined the conformational properties of some dipeptide, tripeptide, tetrapeptide and pentapeptide fragments of hylambatin. The calculation of stable конформационных states of fragments of the molecule has allowed to define the local elements of the secondary structure and energy preferred mutual orientation of residues in stable structures. Calculations showed that C-terminal pentapeptide of hylambatin molecule preferentially adopt the alpha-helical conformation, stabilized by hydrogen bonds between the end groups of molecule. On the base of calculated values of dihedral angles of stable conformations of fragments have been constructed their molecular models.