Conformational Variety of Polyanionic Peptides At Low Salt Concentrations

Details Conformational Variety of Polyanionic Peptides At Low Salt Concentrations Conformational Variety of Polyanionic Peptides At Low Salt Concentrations

Dec 1997

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1997oleb...27..585b&link_type=abstract

Origins of Life and Evolution of the Biosphere, v. 27, Issue 5/6, p. 585-595 (1997).

Physics

2

Scientific paper

Cordially dedicated to Dr. Leslie Orgel on the occasion of his 70th birthday. Sequential oligo- and polypeptides based on glutamic acid and leucine residues have been synthesized. In pure water, they exhibit a random coil conformation. Addition of very small amounts of divalent metallic cations induces the formation of ordered structure in the peptides which remain in solution. Higher salt concentrations precipitate the peptides. Polypeptides with alternating glutamic acid and leucine residues undergo a coil to β-sheet transition in the presence of Ca^2+, Ba^2+, Mn^2+, Co^2+, Zn^2+ and Hg^2+. Addition of Cu^2+ or Fe^3+ induces the formation of an α-helix. Solid amorphous CdS generates water soluble β-sheets, as well. Sequential poly(Leu-Glu-Glu-Leu) adopts an α-helix in the presence of divalent cations. The sequence-dependent conformational diversity was extended to poly(Asp-Leu) and poly(Leu-Asp-Asp-Leu).

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