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Investigates the gramicidin A folding process and determines the intermediates involved during the incorporation of gramicidin A into the channel state in a model membrane environment. Gramicidin A's adoption of various conformations depending on its environment; Conformational transitions to form ion channels in sodium dodecyl sulfate (SDS) micelles.

Investigates Gramicidin-lipid interactions using diacylphosphatidylcholines (PC) containing two identical acyl chains of varying length. Conformation of Gramicidin A (gA); Micellar organization of PC; Fractionation of gA proportional to acyl chain length; Factors affecting channel structure; Reciprocal gramicidin-lipid interactions.

Investigates the structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. Channel-forming antibiotic; Gramicidin family of linear polypeptides; Correlation of amino acid composition; Mixture of nine pantadecapeptides; Monovalent cation transport; Incorporation of the structures into deuterated sodium dodecyl sulfate micelles.