通过平衡透析法估算模型肽与DNA结合的亲和常数。
The estimation of affinity constants for the binding of model peptides to DNA by equilibrium dialysis.
作者信息
Standke K C, Brunnert H
出版信息
Nucleic Acids Res. 1975 Oct;2(10):1839-49. doi: 10.1093/nar/2.10.1839.
Abstract
The binding of lysine model peptides of the type Lys-X-Lys, Lys-X-X-Lys and Lys-X-X-X-Lys (X = different aliphatic and aromatic amino acids) has been studied by equilibrium dialysis. It was shown that the strong electrostatic binding forces generated by protonated amino groups of lysine can be distinguished from the weak forces stemming from neutral and aromatic spacer amino acids. The overall binding strength of the lysine model peptides is modified by these weak binding forces and the apparent binding constants are influenced more by the hydrophobic character of the spacer amino acid side chains than by the chainlength of the spacers.
摘要
通过平衡透析研究了Lys-X-Lys、Lys-X-X-Lys和Lys-X-X-X-Lys类型（X = 不同的脂肪族和芳香族氨基酸）的赖氨酸模型肽的结合情况。结果表明，赖氨酸质子化氨基产生的强静电结合力可与中性和芳香族间隔氨基酸产生的弱作用力区分开来。这些弱结合力改变了赖氨酸模型肽的整体结合强度，表观结合常数受间隔氨基酸侧链疏水特性的影响大于间隔长度的影响。
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