ABSTRACT The spatial structure of the cardioactive peptides Lys1-Asn2-Glu3-Phe4-Ile5-Arg6-Phe7-NH2 (K N E F I R F amide) and Ser1-Asp2-Asn3-Phe4-Met5-Arg6-Phe7-NH2 (S D N F M R F amide) have been investigated using the method of molecular mechanics. The low-energy conformations of these peptide molecules were found, the geometric, energy parameters and stabilizing interaction energies in the optimal conformations of these peptides were determined. It is found that the spatial structure of K N E F I R F amide molecule can exist in nine stable backbone forms and the spatial structure of S D N F M R F amide molecule can exist in eighteen stable backbone forms.
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