Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10797652 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 8 Pages |
Abstract
⺠Helix-2 of TatA is predominantly helical in membrane environments. ⺠Helix-2 of TatA interacts with negatively charged lipids. ⺠Solution structure of the TatA helix-2 peptide shows it forms an amphipathic helix.
Keywords
DSCSDS1,2-dipalmitoyl-sn-glycero-3-phospho-(1′-rac-glycerol)TatAEggPGDPPCDPCEggPCDPPGnuclear magnetic resonance1,2-dipalmitoyl-sn-glycero-3-phosphocholinelarge unilamellar vesiclesTATTwin-arginine translocationtwin-arginine translocaseNMRDodecylphosphocholinecircular dichroismNMR solution structuresodium dodecyl sulfateLUVSUVAmphipathic peptideDifferential scanning calorimetrysmall unilamellar vesicles
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Authors
Catherine S. Chan, Evan F. Haney, Hans J. Vogel, Raymond J. Turner,