Characterization of the interfacial behavior and structure of the signal sequence of Escherichia coli outer membrane pore protein PhoE.
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.
Batenburg
A M
AM
Department of Biochemistry, State University of Utrecht, The Netherlands.
Brasseur
R
R
Ruysschaert
J M
JM
van Scharrenburg
G J
GJ
Slotboom
A J
AJ
Demel
R A
RA
de Kruijff
B
B
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
D001425:Bacterial Outer Membrane Proteins; D010446:Peptide Fragments; D018272:Porins