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Electrostatic Interaction Between Oligopeptides and Phosphate Residues by Determination of Absolute Raman Intensities

机译:寡肽和磷酸残基之间的静电相互作用的绝对拉曼强度测定

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The changed isotropic absolute Raman intensities of the phosphate residue in the complexes of positive charge oligopeptides, lys-lys, arg-arg, lys-aromat-lys, negative charge diethyl phosphoric acid (DEP) and polyriboadenylic acid{poly(rA)} were reported and discussed. Our measurements showed that the absolute intensities of phosphate stretch vibration in complexes were different according to the reaction partners. Due to the partial electrical charge and molecular structure of oligopeptides for the complex formation lysine can interact more strongly than arginine when the reaction partners have short chain and no steric hindrance. Owing to these reasons the intensity of phosphate stretching vibration is very sensitive according to the circumstance of reaction. From our results we could suggest that we can discriminate any one of the the lysine and arginine in the complicated biological molecule during interaction between nucleotides and proteins. The activity of reaction of two basical oligopeptides is not quite similar for complex formation in aqueous solution. The activity of dipeptides depends upon the structure of molecule and environment for complex formation. Aromatic ring contributes to electrostatic interaction in complexes. The amount of the absolute intensity for pure stacking interaction is smaller than electrostatic interaction in macromolecular complexes.
机译:正电荷寡肽,lys-lys,arg-arg,lys-aromat-lys,负电荷二乙基磷酸(DEP)和聚核糖腺苷酸{poly(rA)}的配合物中磷酸酯残基的各向同性绝对拉曼强度变化为报告和讨论。我们的测量结果表明,根据反应伙伴的不同,配合物中磷酸盐拉伸振动的绝对强度会有所不同。由于用于复杂形成的寡肽的部分电荷和分子结构,当反应伙伴具有短链且没有空间位阻时,赖氨酸的相互作用比精氨酸更强。由于这些原因,根据反应情况,磷酸盐拉伸振动的强度非常敏感。根据我们的结果,我们可以认为,在核苷酸和蛋白质相互作用期间,我们可以区分复杂生物分子中的赖氨酸和精氨酸中的任何一种。对于在水溶液中形成复合物,两种碱性寡肽的反应活性不太相似。二肽的活性取决于分子的结构和形成复合物的环境。芳香环有助于复合物中的静电相互作用。纯堆积相互作用的绝对强度小于大分子配合物中的静电相互作用。

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