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- W2039953314 abstract "Random copolymers of lysine and alanine, 2 : 1 and 1 : 1, were trimethylated on the lysine. amino groups to quaternary ammonium groups. Methylated and unmethylated polymers were prepared with Cl− or ClO as the counterion. CD spectra were measured for increasing concentration of peptide without added salt, and at constant peptide concentration in increasing NaCl or NaClO4. Unmethylated peptides, as the chloride, form α-helix more readily than do the methylated peptides. The opposite occurs with ClO as counterion. The helix-promoting effect of methylated lysine residues (ClO counterion) is diminished by the presence of alanine, as compared with effects when lysine is the only type of residue. The effect of methylation of proteins on helix formation may depend on the types of anionic groups with which the protein may be involved." @default.
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- W2039953314 date "1992-05-01" @default.
- W2039953314 modified "2023-09-25" @default.
- W2039953314 title "Helix formation in methylated copolymers of lysine and alanine" @default.
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- W2039953314 doi "https://doi.org/10.1002/bip.360320505" @default.
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