Permiakov E A, Deĭkus G Iu
Mol Biol (Mosk). 1995 Mar-Apr;29(2):339-44.
The well-known conformational changes in proteins containing a single tryptophan residue, such as pH-induced N-->F transition in human serum albumin, pH-induced acidic transition in cod parvalbumin, and KCl-induced tetramerization of bee venom melittin were monitored by changes in low temperature phosphorescence and fluorescence spectra suggesting two independent series of normal components. Parameters of low temperature tryptophan luminescence were sensitive to chromophore environment. A correlation of changes of some spectral parameters with accessibility of tryptophan to water was revealed, however, spectral changes mainly depend on specific interactions of the chromophore with its environment.
含有单个色氨酸残基的蛋白质中众所周知的构象变化，例如人血清白蛋白中pH诱导的N→F转变、鳕鱼小清蛋白中pH诱导的酸性转变以及蜂毒蜂毒肽的KCl诱导的四聚化，通过低温磷光和荧光光谱的变化进行监测，表明存在两个独立的正常组分系列。低温色氨酸发光的参数对发色团环境敏感。揭示了一些光谱参数的变化与色氨酸对水的可及性之间的相关性，然而，光谱变化主要取决于发色团与其环境的特定相互作用。
