Ragone R, Colonna G, Balestrieri C, Servillo L, Irace G
Biochemistry. 1984 Apr 10;23(8):1871-5. doi: 10.1021/bi00303a044.
The mutual interference between the second-derivative bands of tyrosine and tryptophan in proteins has been evaluated in terms of the ratio r between two peak to peak distances. The r values have been found to be not only related to the tyrosine/tryptophan ratio but also dependent on the polarity of the medium in which tyrosyl residues are embedded. The results obtained on purified proteins have been found consistent with the available X-ray information and with the existing solvent perturbation data.
蛋白质中酪氨酸和色氨酸二阶导数谱带之间的相互干扰已根据两个峰峰距离之间的比率r进行了评估。已发现r值不仅与酪氨酸/色氨酸比率有关，还取决于酪氨酸残基所处介质的极性。在纯化蛋白质上获得的结果与现有的X射线信息以及现有的溶剂扰动数据一致。
