Barbucci R, Magnani A, Roncolini C, Silvestri S
Dipartimento di Chimica, Siena, Italy.
Biopolymers. 1991 Jun;31(7):827-34. doi: 10.1002/bip.360310703.
Biotin-avidin recognition is studied by Fourier transform ir spectroscopy/attenuated total reflection (FTIR/ATR) under physiological conditions. The ureido portion of biotin is confirmed to be involved in the interaction with avidin, as previously found, but when the biotin-avidin complex forms, an electrostatic interaction occurs between the carboxylate group of the biotin molecule and the protonated aminic end group of the avidin amino acid side chains. Comparison of the biotin-avidin system with the biotin-1,4-diaminobutane and biotin-tryptophan systems confirms these findings.
在生理条件下,通过傅里叶变换红外光谱/衰减全反射(FTIR/ATR)研究生物素-抗生物素蛋白的识别。如先前发现的那样,生物素的脲基部分确实参与了与抗生物素蛋白的相互作用,但是当生物素-抗生物素蛋白复合物形成时,生物素分子的羧基与抗生物素蛋白氨基酸侧链的质子化氨基端基之间会发生静电相互作用。将生物素-抗生物素蛋白系统与生物素-1,4-二氨基丁烷和生物素-色氨酸系统进行比较证实了这些发现。