title: Characterization of the interfacial behavior and structure of the signal sequence of Escherichia coli outer membrane pore protein PhoE.
abstract: The behavior of the chemically synthesized PhoE signal peptide and signal peptide fragments on hydrophilic-hydrophobic interfaces was studied with circular dichroism and monolayer techniques. The experimental results were compared with computer-calculated predictions of peptide structure, orientation, and molecular area. The complete signal sequence was found to aggregate in a beta-sheet structure when introduced in an aqueous environment; on the other hand, in sodium dodecyl sulfate micelles approximately 75% alpha-helical structure was observed. Assuming this to reflect the actual structure in a peptide monolayer and taking into account the orientations predicted for the fragments, the measured molecular areas suggest a looped orientation of the signal sequence with both N and C terminus in the water phase.
authors.affiliation: Department of Biochemistry, State University of Utrecht, The Netherlands.
authors.forename: A M
authors.initials: AM
authors.lastname: Batenburg
authors.forename: R
authors.initials: R
authors.lastname: Brasseur
authors.forename: J M
authors.initials: JM
authors.lastname: Ruysschaert
authors.forename: G J
authors.initials: GJ
authors.lastname: van Scharrenburg
authors.forename: A J
authors.initials: AJ
authors.lastname: Slotboom
authors.forename: R A
authors.initials: RA
authors.lastname: Demel
authors.forename: B
authors.initials: B
authors.lastname: de Kruijff
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000032:analysis*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis*; D018272:Porins; D011312:Pressure; D011487:Protein Conformation
chemical_list: D001425:Bacterial Outer Membrane Proteins; D010446:Peptide Fragments; D018272:Porins