Effect of intrachain hydrogen bond on the formation of L amino acids along α helix of peptide

【摘要】 <正> The model of right-handed α helix of peptide,in which the intrachain hydrogen bonds be-tween amino acid residues are in the direction of the axis of the helix,is used to compute the energy differ-ences between D-and L-form residues.The dominant intramolecular interactions involved are the Coulombinteraction for the residues with charged and polarized R group and van der Waals interaction for thehydrophobic residues respectively.The results obtained show that the energy states of L-forms are lower thanthose of the corresponding D-forms.Therefore,L-form states are more stable.The racemization of the aminoacid after the residue has been dislocated from the peptide chain is interpreted as the consequence of the pari-ty conservation of the electromagnetic interaction.更多还原

【Abstract】 The model of right-handed α helix of peptide,in which the intrachain hydrogen bonds be- tween amino acid residues are in the direction of the axis of the helix,is used to compute the energy differ- ences between D-and L-form residues.The dominant intramolecular interactions involved are the Coulomb interaction for the residues with charged and polarized R group and van der Waals interaction for the hydrophobic residues respectively.The results obtained show that the energy states of L-forms are lower than those of the corresponding D-forms.Therefore,L-form states are more stable.The racemization of the amino acid after the residue has been dislocated from the peptide chain is interpreted as the consequence of the pari- ty conservation of the electromagnetic interaction.更多还原