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MARYE ANNE FOX Department of Chemistry University of Texas Austin The design of short monomeric peptides with stable helical secondary structure can be achieved by complexation with ap- propriate metal ions. The unusual stability of the resulting helix may relate to the enhanced entropy of the cross-linked peptide. F.Q. Ruan, Y.Q. Chen, P.B. Hopkins, "Metal ion enhanced helicity in synthetic peptides containing unnatural, metal-ligating residues," Journal of the American Chemical Society (J

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MARYE ANNE FOX
Department of Chemistry
University of Texas Austin

The design of short monomeric peptides with stable helical secondary structure can be achieved by complexation with ap- propriate metal ions. The unusual stability of the resulting helix may relate to the enhanced entropy of the cross-linked peptide.

F.Q. Ruan, Y.Q. Chen, P.B. Hopkins, "Metal ion enhanced helicity in synthetic peptides containing unnatural, metal-ligating residues," Journal of the American Chemical Society (JACS), 112, 9403-4, 5 December 1990. (University of Washington, Seattle) M.R. Ghadiri, A.K. Fernholz, "Peptide architecture. Design of stable a-helical metallopeptides via a novel exchange-inert Ru(III) complex," JACS, 112, 9633-5, 19 December 1990. (Research Institute of Scripps Clinic, La Jolla, Calif.)

Mechanistic details define aggregation equilibria in organomagnesium nucleophiles and intramolecular assistance by ligands in stabilizing the transition states of these transformations.

K.A. Swiss, D.C. Liotta, C.A. Maryanoff, "Mechanistic aspects of the ligand-assisted nucleophilic addition reaction," JACS, 112, 9393-4, ...

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