- Abstract:
-
A 28-mer peptide (gammaM4) corresponding to the fourth transmembrane segment of the nicotinic acetylcholine receptor (AChR) gamma-subunit, with a single tryptophan residue (Trp6), was reconstituted into lipid bilayers of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), loaded with either high or low amounts of cholesterol, i.e., in the conjugated liquid-ordered and liquid-disordered phases, respectively, at room temperature. By making use of the Trp intrinsic fluorescence, both steady...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1080/09687860600703613
-
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- Journal:
- Molecular membrane biology
- Volume:
- 23
- Issue:
- 4
- Pages:
- 305-315
- Publication date:
- 2006-01-01
- DOI:
- EISSN:
-
1464-5203
- ISSN:
-
0968-7688
- URN:
-
uuid:8b3b64c6-1155-4e57-b6d9-0235fe583efd
- Source identifiers:
-
100452
- Local pid:
- pubs:100452
- Copyright date:
- 2006
Journal article
Structure and dynamics of the gammaM4 transmembrane domain of the acetylcholine receptor in lipid bilayers: insights into receptor assembly and function.
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