Sogami M, Era S, Nagaoka S, Inouye H
Int J Pept Protein Res. 1982 Mar;19(3):263-9. doi: 10.1111/j.1399-3011.1982.tb03037.x.
The acid-induced isomerization (the N-F transition) and expansion of bovine plasma albumin were studied by measuring circular dichroic spectra and fluorescence polarization of tryptophyl residues. Decreases in the magnitude of ellipticities at 208, 222, 262 and 268 nm were observed in the N-F transition and acid-expansion. However, increases in the magnitude of ellipticities at 295-300 nm observed in the initial part of the N-F transition exactly correlated with the increase of rotational relaxation time of tryptophyl side chains obtained by fluorescence polarization measurement.
通过测量牛血清白蛋白的圆二色光谱和色氨酸残基的荧光偏振，研究了酸诱导的异构化（N-F转变）和膨胀。在N-F转变和酸膨胀过程中，观察到208、222、262和268nm处椭圆率的大小降低。然而，在N-F转变初始阶段观察到的295-300nm处椭圆率大小的增加与通过荧光偏振测量得到的色氨酸侧链旋转弛豫时间的增加完全相关。
