| 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
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Catherine S. Chan, Evan F. Haney, Hans J. Vogel, Raymond J. Turner,