Schlyer B D, Maki A H, Hawrot E
Department of Chemistry, University of California, Davis 95616.
FEBS Lett. 1992 Feb 3;297(1-2):87-90. doi: 10.1016/0014-5793(92)80333-c.
Phosphorescence and optically detected magnetic resonance (ODMR) have been used to characterize two synthetic peptides, alpha 181-198 and alpha 185-196, of the major binding determinant of the alpha-acetylcholine receptor (AChR) of Torpedo californica and its interaction with alpha-bungarotoxin (BgTX) using Trp as an intrinsic probe. BgTX conformational changes are suggested upon complexation with the peptides. Methylmercury-modified peptides show conformational heterogeneity which brings some of the modified Cys residues into proximity of peptide Trp(s). These modified peptides, when bound to BgTX, undergo structural changes which remove the tagged Cys from its close contact with the Trp residue(s) of the peptide.
磷光和光探测磁共振（ODMR）已被用于表征来自加州电鳐α-乙酰胆碱受体（AChR）主要结合决定簇的两种合成肽α181 - 198和α185 - 196，以及使用色氨酸作为内在探针研究它们与α-银环蛇毒素（BgTX）的相互作用。提示BgTX与肽络合时会发生构象变化。甲基汞修饰的肽表现出构象异质性，这使得一些修饰的半胱氨酸残基靠近肽的色氨酸。这些修饰的肽与BgTX结合时会发生结构变化，使标记的半胱氨酸不再与肽的色氨酸残基紧密接触。
