Differences in the hydrophobic properties of discrete alpha-helical domains of rat and human apolipoprotein A-IV
- 1 April 1987
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
- Vol. 918 (3) , 299-303
- https://doi.org/10.1016/0005-2760(87)90234-7
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Isolation and lipid-binding properties of rat apolipoprotein A-IVBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1985
- Rat apolipoprotein A-IV contains 13 tandem repetitions of a 22-amino acid segment with amphipathic helical potential.Proceedings of the National Academy of Sciences, 1984
- The helical hydrophobic moment: a measure of the amphiphilicity of a helixNature, 1982
- The redistribution and metabolism of iodinated apolipoprotein A-IV in ratsBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1980
- Human Apolipoprotein A-IVJournal of Clinical Investigation, 1980
- Apolipoprotein A‐IV: a Protein Occurring in Human Mesenteric Lymph Chylomicrons and Free in PlasmaEuropean Journal of Biochemistry, 1979
- Surface and inside volumes in globular proteinsNature, 1979
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Characterization of the apolipoproteins of rat plasma lipoproteinsBiochemistry, 1977
- A simplified representation of protein conformations for rapid simulation of protein foldingJournal of Molecular Biology, 1976