Beta-structures of polypeptides with L-and D-residues. Part II. Statistical analysis and enrichment in enantiomer.
The possible formation of beta-structures from polypeptide chains with L-and D-Residues randomly distributed was statistically analyzed within the frame of two hypotheses. Firstly, only those segments containing residues of identical chirality can associate to form antiparallel beta-structures, and secondly these segments must have a minimum length. The influence of different factors was examined: initial ratio of the L-and D-monomer, minimum length required for the segments to be incorporated into beta-sheets, average length of the peptide molecules, and stereoselectivity in the course of the polymerization process. The results show that in all cases nuclei of beta-sheets surrounded by random coil segments are formed, the optical activity of which very increases to purity when the initial ratio of monomers deviates from the racemic mixture. This suggests experiments to enrich the system in one enantiomer. Comparison is made with the corresponding behavior and properties of the alpha-helical structure.
D007536:Isomerism; D008433:Mathematics; D010455:Peptides; D011487:Protein Conformation; D013223:Statistics as Topic; D013329:Structure-Activity Relationship
D010455:Peptides