Jhon N I, Casas-Finet J R, Maki A H, Modrich P
Department of Chemistry, University of California, Davis 95717.
Biochim Biophys Acta. 1988 Feb 28;949(2):189-94. doi: 10.1016/0167-4781(88)90082-6.
The binding of EcoRI endonuclease to the oligonucleotides d(GCGAATTCGC) and d(GCGAA) (5BrdU) (5BrdU) d(CGC) has been investigated to determine whether stacking interactions occur between tryptophan residues and the DNA bases. Fluorescence binding isotherms show that the decamer containing the canonical and that containing the modified recognition sequence bind with comparable affinity. Optically detected magnetic resonance spectra show limited perturbations of the Trp zero-field splitting parameters, which are assigned to electrical field effects. No evidence for Trp stacking interactions has been found.
为了确定色氨酸残基与DNA碱基之间是否发生堆积相互作用，对EcoRI核酸内切酶与寡核苷酸d(GCGAATTCGC)和d(GCGAA)(5-溴尿嘧啶)(5-溴尿嘧啶)d(CGC)的结合进行了研究。荧光结合等温线表明，含有标准序列的十聚体和含有修饰识别序列的十聚体以相当的亲和力结合。光探测磁共振光谱显示色氨酸零场分裂参数的扰动有限，这归因于电场效应。未发现色氨酸堆积相互作用的证据。
