Glutamic acid, conformation

Peculiar DNA architecture was demonstrated in 25% aqueous ethanol when DNA was complexed with series of cationic detergents in the presence of poly(glutamic acid) [124]. Electron microscopy and x-ray scattering demonstrated that DNA can pack cetyltrimethylammonium bromide molecules into rodlike micelles, which form a hexagonal lattice. Interestingly, circular dichroism spectroscopy revealed that in these complexes DNA adopts left-handed conformation. 

Amphipathic peptides contain amino acid sequences that allow them to adopt membrane active conformations [219]. Usually amphipathic peptides contain a sequence with both hydrophobic amino acids (e.g., isoleucine, valine) and hydrophilic amino acids (e.g., glutamic acid, aspartic acid). These sequences allow the peptide to interact with lipid bilayer. Depending on the peptide sequence these peptides may form a-helix or j6-sheet conformation [219]. They may also interact with different parts of the bilayer. Importantly, these interactions result in a leaky lipid bilayer and, therefore, these features are quite interesting for drug delivery application. Obviously, many of these peptides are toxic due to their strong membrane interactions. 

Fig. 3. Backscattered Raman (/R + /L) and ROA (/R — /L) spectra of poly-L-lysine in o -helical (top pair) and disordered (second pair) conformations, and of poly-L-glutamic acid in a-helical (third pair) and disordered (bottom pair) conformations in aqueous solution. Reprinted from Barron et al., 2000, Prog. Biophys. Mol. Biol. 73, 1-49, with permission from Elsevier Science.

Aspartic and glutamic acids are themselves negatively charged under physiological conditions. This allows them to chelate certain metal ions, and also to markedly influence the conformation adopted by polypeptide chains in which they are found. 

N 022 "Conformational Analysis of Macromolecules. V. Helical Structures of PolylL-aspartic acid) and PolylL-glutamic acid), and Related Compounds"... 

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