Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids. Evidence for the snorkel hypothesis.
Open Access
- 1 March 1994
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (10) , 7185-7191
- https://doi.org/10.1016/s0021-9258(17)37266-6
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Luminescence studies with trp repressor and its single-tryptophan mutantsBiochemistry, 1993
- Colicin Ia inserts into negatively charged membranes at low pH with a tertiary but little secondary structural changeBiochemistry, 1993
- Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptideBiochemistry, 1992
- Minimal peptide length for interaction of amphipathic .alpha.-helical peptides with phosphatidylcholine liposomesBiochemistry, 1991
- Shielding of tryptophan residues of avidin by the binding of biotinBiochemistry, 1989
- In vitro binding of synthetic acylated lipid-associating peptides to high-density lipoproteins: effect of hydrophobicityBiochemistry, 1984
- Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescenceBiochemistry, 1983
- A molecular theory of lipid—protein interactions in the plasma lipoproteinsFEBS Letters, 1974
- Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholineBiochemistry, 1973
- The use of sequestering agents in the preparation of ε-Acyl-L-lysine and δ-Acyl-L-ornithine derivativesAustralian Journal of Chemistry, 1965