Amphipathic helixes and plasma lipoproteins: A computer study
- 1 September 1977
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 16 (9) , 2053-2065
- https://doi.org/10.1002/bip.1977.360160916
Abstract
A molecular model for the lipid‐associating domains of the A and C plasma apolipoproteins was recently proposed. This model consists of helical regions with special properties termed amphipathic. In the present communication we present a computer analysis of the general occurrence of amphipathic helix patterns in proteins with known amino acid sequences.This publication has 13 references indexed in Scilit:
- Amphipathic helixes and plasma lipoproteins: Thermodynamic and geometric considerationsChemistry and Physics of Lipids, 1977
- Molecular packing of high density lipoproteins: A postulated functional roleFEBS Letters, 1976
- The Primary Structure of High Density Apolipoprotein-Glutamine-IProceedings of the National Academy of Sciences, 1974
- 13 C Nuclear Magnetic Resonance Spectroscopic Evidence for Hydrophobic Lipid-Protein Interactions in Human High Density LipoproteinsProceedings of the National Academy of Sciences, 1974
- Membrane proteins: Amino acid sequence and membrane penetrationJournal of Molecular Biology, 1974
- A molecular theory of lipid—protein interactions in the plasma lipoproteinsFEBS Letters, 1974
- A STATISTICAL ANALYSIS OF THE AMINO ACID COMPOSITIONS OF PROTEINSInternational Journal of Peptide and Protein Research, 1973
- Identification of the abnormal cholestatic lipoprotein (LP‐X) in familial lecithin:Cholesterol acyltransferase deficiencyFEBS Letters, 1972
- Amino Acid Sequence of Human apoLp-Gln-II (apoA-II), an Apolipoprotein Isolated from the High-Density Lipoprotein ComplexProceedings of the National Academy of Sciences, 1972
- Structure and function of haemoglobinJournal of Molecular Biology, 1965