Examination of phenylalanine microenvironments in proteins by second-derivative absorption spectroscopy.
Examination of phenylalanine microenvironments in proteins by second-derivative absorption spectroscopy.
复制标题
通过二阶导数吸收光谱检查蛋白质中的苯丙氨酸微环境。
DOI：
10.1016/0003-9861(91)90384-u
复制
发表时间：
1991
影响因子：
3.9
通讯作者：
Lewis,RV
中科院分区：
文献类型：
--
作者：
Mach,H;Thomson,JA;Middaugh,CR;Lewis,RV
We have employed near ultraviolet derivative absorption spectroscopy to study the microenvironments of phenylalanine residues in proteins. The use of second-derivative uv spectra in the 250- to 270-nm range effectively suppresses spectral contributions from tryptophan and tyrosine residues. Fitting a polynomial to the numerically calculated second-derivative spectrum allows precise determination of the position of the negative derivative peak near 258 nm. This position is shown to be correlated with the polarity of the microenvironments of phenylalanine residues. This approach allows monitoring of changes in the state of phenylalanine side chains during folding/unfolding of the proteins. In addition, this method permits perturbation of protein samples with ethylene glycol to be used to establish the relative degree of solvent exposure of protein phenylalanine.
