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Abstract
Gene 9 protein is one of the minor coat proteins of bacteriophage M13. The protein plays a role in the assembly process by associating with the host membrane by protein-lipid interactions. The availability of chemically synthesized protein has enabled the biophysical characterization of the membrane-bound state of the protein by using model membrane systems. This paper summarizes, discusses and further interprets this work in the light of the current state of the literature, leading to new possible models of the coat protein in a membrane. The biological implications of these findings related to the membrane-bound phage assembly are indicated.
ATR-FTIR, Attenuated total reflectance-Fourier transform infrared; CD, circular dichroism; DOPC, Di18C:1Δ9c PC (dioleoyl-PC); DOPG, Di18C:1Δ9c PG (dioleoyl-PG); FTIR, Fourier transform infrared; HPSEC, High performance size exclusion chromatography; PC, Phosphatidylcholine; PG, Phosphatidylglycerol; SDS, Sodium dodecyl sulphate; TFE, Trifluoroethanol
ATR-FTIR, Attenuated total reflectance-Fourier transform infrared; CD, circular dichroism; DOPC, Di18C:1Δ9c PC (dioleoyl-PC); DOPG, Di18C:1Δ9c PG (dioleoyl-PG); FTIR, Fourier transform infrared; HPSEC, High performance size exclusion chromatography; PC, Phosphatidylcholine; PG, Phosphatidylglycerol; SDS, Sodium dodecyl sulphate; TFE, Trifluoroethanol