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Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2014 Jan; Vol. 1838 (1 Pt B), pp. 413-8. Date of Electronic Publication: 2013 Oct 19. - Publication Year :
- 2014
-
Abstract
- The chloroplast twin arginine translocation (cpTat) system transports highly folded precursor proteins into the thylakoid lumen using the protonmotive force as its only energy source. Hcf106, as one of the core components of the cpTat system, is part of the precursor receptor complex and functions in the initial precursor-binding step. Hcf106 is predicted to contain a single amino terminal transmembrane domain followed by a Pro-Gly hinge, a predicted amphipathic α-helix (APH), and a loosely structured carboxy terminus. Hcf106 has been shown biochemically to insert spontaneously into thylakoid membranes. To better understand the membrane active capabilities of Hcf106, we used solid-state NMR spectroscopy to investigate those properties of the APH. In this study, synthesized peptides of the predicted Hcf106 APH (amino acids 28-65) were incorporated at increasing mol.% into 1-palmitoyl-2-oleoyl-sn-glycero-phosphocholine (POPC) and POPC/MGDG (monogalactosyldiacylglycerol; mole ratio 85:15) multilamellar vesicles (MLVs) to probe the peptide-lipid interaction. Solid-state (31)P NMR and (2)H NMR spectroscopic experiments revealed that the peptide perturbs the headgroup and the acyl chain regions of phospholipids as indicated by changes in spectral lineshape, chemical shift anisotropy (CSA) line width, and (2)H order SCD parameters. In addition, the comparison between POPC MLVs and POPC/MGDG MLVs indicated that the lipid bilayer composition affected peptide perturbation of the lipids, and such perturbation appeared to be more intense in a system more closely mimicking a thylakoid membrane.<br /> (© 2013.)
- Subjects :
- Amino Acid Sequence
Magnetic Resonance Spectroscopy methods
Models, Biological
Molecular Sequence Data
Peptides chemical synthesis
Protein Structure, Secondary
Protein Structure, Tertiary
Thylakoids chemistry
Galactolipids chemistry
Lipid Bilayers chemistry
Membrane Proteins chemistry
Peptides chemistry
Phosphatidylcholines chemistry
Plant Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1838
- Issue :
- 1 Pt B
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 24144541
- Full Text :
- https://doi.org/10.1016/j.bbamem.2013.10.007