Structure of a methionine-rich segment of Escherichia coli Ffh protein

Abstract

The methionine-rich segments of the Ffh protein of Escherichia coli and its eukaryotic counterpart SRP54 are thought to bind signal sequences of secretory proteins. The structure of a chemically synthesized 25-residue-long peptide corresponding to one of the proposed methionine-rich amphiphilic helices of Ffh was determined in water and in aqueous trifluroethanol (TFE) solution using CD and NMR. An appreciable alpha-helix conformation exists even in water and this peptide assumes a stable alpha-helix along most of its length in aqueous TFE solution, It is clear that this segment of Ffh protein has a very strong propensity to form alpha-helical structure.