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 theory

Edward M. Kosower

doi:10.1016/0014-5793(82)80613-3

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 theory

Edward M. Kosower^*

^*Corresponding author for this work

School of Chemistry

Stony Brook University

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Four transmembrane segments from each of the β-, γ- and δ-protein subunits of the acetylcholine receptor (AChR) [Nature (1983) 301, 251-255], [Proc. Natl. Acad. Sci. USA (1983) 80, 1111-1115] have been selected on the basis of single group rotation (SGR) theory [Symp. Structure and Dynamics of Nucleic Acids and Proteins (Sept. 1982) abst. pp.52-53], [Biochem. Biophys. Res. Commun. (1983) 111, 1022-1029] and the hydrophobicity of amino acid sequences. One helix from each subunit is assigned to the AChR ion channel. Criteria for the selection of ion channel elements are outlined.

Original language	English
Pages (from-to)	245-247
Number of pages	3
Journal	FEBS Letters
Volume	155
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(82)80613-3
State	Published - 8 May 1983

Keywords

Acetylcholine receptor
Amino acid hydrophobicity
Ion channel location
Single group rotation
Subunit β,γ,δ
Tertiary structure

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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 theory

Abstract

Keywords

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