Effects of backbone modification on helical peptides: the reduced carbonyl modification.
Reducing a CO to a CH2 moiety in a peptide bond destroys the ability of the peptide link to act as a proton acceptor in a hydrogen-bonded structure. Here, this modification is introduced into different positions of the helical peptide, acetyl-WGG(RAAAA)4R-amide, and the melting of these peptides is followed using CD. Effects of this modification on helical peptides are compared to our previous N-methylation studies [C. F. Chang and M. H. Zehfus (1996) Biopolymers, Vol. 40, pp. 609-616]. While the experiments were designed to remove the same hydrogen bond from the peptide, no consistent results are obtained between these two modifications. This result suggests that these modifications not only break the backbone hydrogen bonds, but also involve other destabilizing effects. When our data is analyzed using different helix-coil transition models, the results show that as the models increase in complexity the energy associated with a single residue modification increases. Unfortunately, the most detailed dichroic model, which should best describe this system, works for only one peptide. Apparently, the models need to be further improved to better mimic our system.
Division of Structural Biology, Institute of Biomedical Sciences, Academia Sinca, Taipei, Taiwan, ROC.
C F
CF
Chang
M H
MH
Zehfus
D000595:Amino Acid Sequence; D001704:Biopolymers / Q000737:chemistry; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D001704:Biopolymers; D010455:Peptides