Functional differentiation of amphiphilic helices of the apolipoproteins by hydrophobic moment analysis
- 5 January 1987
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 911 (1), 45-52
- https://doi.org/10.1016/0167-4838(87)90268-8
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- [44] Rat apolipoprotein A-IV: Application of computational methods for studying the structure, function, and evolution of a proteinMethods in Enzymology, 1986
- THREE-DIMENSIONAL STRUCTURE OF MEMBRANE AND SURFACE PROTEINSAnnual Review of Biochemistry, 1984
- [47] Establishing homologies in protein sequencesMethods in Enzymology, 1983
- The helical hydrophobic moment: a measure of the amphiphilicity of a helixNature, 1982
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- PHOSPHOLIPID BINDING STUDIES WITH SYNTHETIC APOLIPOPROTEIN FRAGMENTS *Annals of the New York Academy of Sciences, 1980
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Prediction of chain turns in globular proteins on a hydrophobic basisNature, 1978
- A molecular theory of lipid—protein interactions in the plasma lipoproteinsFEBS Letters, 1974
- Use of Helical Wheels to Represent the Structures of Proteins and to Identify Segments with Helical PotentialBiophysical Journal, 1967