Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl phosphatidylcholine.
Open Access
- 1 August 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (18) , 10248-10255
- https://doi.org/10.1016/s0021-9258(17)39238-4
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopyBiochemistry, 1984
- Calorimetric study of peptide-phospholipid interactions: the glucagon-dimyristoylphosphatidylcholine complexBiochemistry, 1981
- Apolipoprotein A-II: chemical synthesis and biophysical properties of three peptides corresponding to fragments in the amino-terminal halfBiochemistry, 1979
- Mechanism of lipid-protein interaction in the plasma lipoproteins: lipid-binding properties of synthetic fragments of apolipoprotein A-IIBiochemistry, 1977
- Amphipathic helixes and plasma lipoproteins: A computer studyBiopolymers, 1977
- Repeated helical pattern in apolipoprotein-A-INature, 1977
- Amphipathic helixes and plasma lipoproteins: Thermodynamic and geometric considerationsChemistry and Physics of Lipids, 1977
- Lipid—protein interaction in porcine high‐density (HDL3) lipoproteinFEBS Letters, 1975
- A molecular theory of lipid—protein interactions in the plasma lipoproteinsFEBS Letters, 1974
- Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholineBiochemistry, 1973