Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor.
- 1 January 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (1) , 155-159
- https://doi.org/10.1073/pnas.81.1.155
Abstract
Fourier analysis of the hydrophobicities of the acetylcholine receptor subunit sequences reveals regions of amphipathic secondary structure. Prediction of a consensus secondary structure based on this analysis and on an empirical prediction method leads to a testable hypothesis about how the ion channel is formed and might function. Knowledge of the 3-dimensional structure of acetylcholine receptors is consistent with features of the model proposed and provides some constraints.Keywords
This publication has 35 references indexed in Scilit:
- Partial tertiary structure assignments for the β‐, γ‐ and δ‐ subunits of the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theoryFEBS Letters, 1983
- Partial tertiary structure assignment for the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theoryBiochemical and Biophysical Research Communications, 1983
- Periodic features in the amino acid sequence of nematode myosin rodJournal of Molecular Biology, 1983
- The permeability of the endplate channel to organic cations in frog muscle.The Journal of general physiology, 1980
- Immunospecific identification and three-dimensional structure of a membrane-bound acetylcholine receptor from Torpedo californicaJournal of Molecular Biology, 1979
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- Structural studies of a membrane-bound acetylcholine receptor from Torpedo californicaJournal of Molecular Biology, 1977
- The 14-fold periodicity in α-tropomyosin and the interaction with actinJournal of Molecular Biology, 1976
- On the conformation of the acetylcholine receptor protein from Torpedo nobilianaFEBS Letters, 1974
- Tests for comparing related amino-acid sequences. Cytochrome c and cytochrome c551Journal of Molecular Biology, 1971