Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism

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2005
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Ramakrishnan, Muthu
Qu, Jian
Pocanschi, Cosmin L.
Marsh, Derek
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Biochemistry. 2005, 44(9), pp. 3515-3523. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi047603y
Zusammenfassung

The outer-membrane proteins OmpA and FhuA of Escherichia coli are monomeric β-barrels of widely differing size. Polarized attenuated totalreflection infrared spectroscopy has been used to determine the orientation of the β-barrels in phosphatidylcholine host matrices of different lipid chain lengths. The linear dichroism of the amide I band from OmpA and FhuA in hydrated membranes generally increases with increasing chain length from diC(12:0) to diC(17:0) phosphatidylcholine, in both the fluid and gel phases. Measurements of the amide I and amide II dichroism from dry samples are used to deduce the strand tilt (β) 46° for OmpA and β = 44.5° for FhuA). These values are then used to deduce the order parameters, P2(cos α) , of the β-barrels from the amide I dichroic ratios of the hydrated membranes. The orientational ordering of the β-barrels and their assembly in the membrane are discussed in terms of hydrophobic matching with the lipid chains.

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ISO 690RAMAKRISHNAN, Muthu, Jian QU, Cosmin L. POCANSCHI, Jörg KLEINSCHMIDT, Derek MARSH, 2005. Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism. In: Biochemistry. 2005, 44(9), pp. 3515-3523. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi047603y
BibTex
@article{Ramakrishnan2005Orien-8130,
  year={2005},
  doi={10.1021/bi047603y},
  title={Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism},
  number={9},
  volume={44},
  issn={0006-2960},
  journal={Biochemistry},
  pages={3515--3523},
  author={Ramakrishnan, Muthu and Qu, Jian and Pocanschi, Cosmin L. and Kleinschmidt, Jörg and Marsh, Derek}
}
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