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- Title
Proton-decoupled <sup>15</sup>N and <sup>31</sup>P solid-state NMR investigations of the Pf3 coat protein in oriented phospholipid bilayers.
- Authors
Aisenbrey, Christopher; Harzer, Ulrike; Bauer-Manz, Gabriele; Bär, Gerda; Chotimah, Irma N. Husnal; Bertani, Philippe; Sizun, Christina; Kuhn, Andreas; Bechinger, Burkhard
- Abstract
The coat proteins of filamentous phage are first synthesized as transmembrane proteins and then assembled onto the extruding viral particles. We investigated the transmembrane conformation of the Pseudomonas aeruginosa Pf3 phage coat protein using proton-decoupled 15N and 31P solid-state NMR spectroscopy. The protein was either biochemically purified and uniformly labelled with 15N or synthesized chemically and labelled at specific sites. The proteins were then reconstituted into oriented phospholipid bilayers and the resulting samples analysed. The data suggest a model in which the protein adopts a tilted helix with an angle of ≈ 30° and an N-terminal ‘swinging arm’ at the membrane surface.
- Subjects
FILAMENTOUS fungi; PSEUDOMONAS aeruginosa; PSEUDOMONAS; BILAYER lipid membranes; PROTEINS; BACTERIA; SPECTRUM analysis
- Publication
FEBS Journal, 2006, Vol 273, Issue 4, p817
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2006.05114.x