Khamis M I, Casas-Finet J R, Maki A H, Murphy J B, Chase J W
FEBS Lett. 1987 Jan 26;211(2):155-9. doi: 10.1016/0014-5793(87)81427-8.
Fluorescence and optical detection of triplet state magnetic resonance spectroscopy have been employed to study the complexes formed by single-stranded polynucleotides with both E. coli single-stranded DNA-binding protein and an E. coli ssb gene product in which Trp-54 is replaced by phenylalanine using site specific oligonucleotide mutagenesis. Our results strongly suggest the involvement of Trp-54 in stabilizing the protein-nucleic acid complexes via stacking interactions of the aromatic residue with the nucleotide bases.
已采用三重态磁共振光谱的荧光和光学检测方法,来研究单链多核苷酸与大肠杆菌单链DNA结合蛋白以及通过位点特异性寡核苷酸诱变使色氨酸-54被苯丙氨酸取代的大肠杆菌单链结合蛋白基因产物所形成的复合物。我们的结果有力地表明,色氨酸-54通过芳香族残基与核苷酸碱基的堆积相互作用参与稳定蛋白质-核酸复合物。