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Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy.
Biochem J. 1992 Dec 1;288 ( Pt 2)(Pt 2):421-6. doi: 10.1042/bj2880421.
Biochem J. 1992.
PMID: 1463446
Free PMC article.
The temperature-dependence of the i.r. spectrum indicates a massive loss of ordered protein structure, occurring at temperatures similar to those reported for thermal denaturation of the AcChR by differential scanning calorimetry and by thermal inactivation of alpha-bungarotoxin- …
The temperature-dependence of the i.r. spectrum indicates a massive loss of ordered protein structure, occurring at temperatures similar to …
Thermal perturbation studies of membrane-bound acetylcholine receptor from Torpedo: effects of cholinergic ligands and membrane perturbants.
Artigues A, Villar MT, Ferragut JA, Gonzalez-Ros JM.
Artigues A, et al.
Arch Biochem Biophys. 1987 Oct;258(1):33-41. doi: 10.1016/0003-9861(87)90319-5.
Arch Biochem Biophys. 1987.
PMID: 3662540
The information obtained from differential scanning calorimetry (DSC) of AcChR membranes (M.C. Farach and M. Martinez-Carrion (1983) J. Biol. Chem. 258, 4176) in the absence and in the presence of cholinergic ligands and local anesthetics, is comparable to that obtained fr …
The information obtained from differential scanning calorimetry (DSC) of AcChR membranes (M.C. Farach and M. Martinez-Carrion (1983) J. Biol …
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