Filippi B, Borin G, Moroder L, Marchiori F
Biochim Biophys Acta. 1976 Dec 13;454(3):514-23. doi: 10.1016/0005-2787(76)90277-x.
Near-ultraviolet difference absorption and circular dichroism (CD) spectra were recorded upon recombination of synthetic S-peptide analogs, i.e. 1epsilon, 7epsilon-diguanidino-[Tyr8]-,1epsilon,7epsilon-diguanidono-[Asn14]-, [Phe(F)8, Orn10]- and 1epsilon, 7epsilon-diguanidino-S-peptide, with S-protein. Environmental alterations of Phe-8 in the S-peptide and Tyr-25 in the S-protein, derived from the association process, lead to strong optical signals whose location and magnitude were clearly defined by means of a comparative analysis of the above spectra. Additionally, the spectroscopic effects resulting from insertion of a tyrosyl residue into an hydrophobic environment in the presence or absence of hydrogen-bonding partners were identified and compared with similar findings obtained from the model compound p-cresol.
在合成的S-肽类似物，即1ε,7ε-二胍基-[Tyr8]-、1ε,7ε-二胍基-[Asn14]-、[Phe(F)8,Orn10]-和1ε,7ε-二胍基-S-肽与S-蛋白重组时，记录了近紫外差吸收光谱和圆二色性（CD）光谱。由缔合过程引起的S-肽中Phe-8和S-蛋白中Tyr-25的环境变化导致了强烈的光学信号，通过对上述光谱的对比分析明确了其位置和强度。此外，还确定了在存在或不存在氢键伙伴的情况下，将酪氨酰残基插入疏水环境所产生的光谱效应，并与从模型化合物对甲酚获得的类似结果进行了比较。
