Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism.
Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism.
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基于一级序列和圆二色性的载脂蛋白A-I和E-3的构象分析。
DOI：
10.1016/s0006-3495(92)81698-3
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发表时间：
1992
影响因子：
3.4
通讯作者：
Atkinson,D
中科院分区：
文献类型：
--
作者：
Nolte,RT;Atkinson,D
本文对人血浆载脂蛋白A-I和载脂蛋白E-3的一级和二级结构进行了分析，以进一步了解这些蛋白质的二级和三级构象以及血浆脂蛋白颗粒的结构和功能。用于分析这些蛋白质的一级序列的方法使用计算机程序：（a）基于每个残基的物理化学性质内的保守取代和相似性来鉴定这些蛋白质内的重复模式;（B）用于物理化学性质的局部平均、疏水矩和傅立叶分析;和（c）使用基于同源性、统计学和信息论的方法进行每种蛋白质的二级结构预测。圆二色谱用于研究纯化的脂质-蛋白质复合物的每种蛋白质和定量的二级结构在脂质环境中。将这些分析的数据整合到单个二级结构预测中，以推导出每种蛋白质的模型。载脂蛋白A-I、E-3和A-IV内的序列同源性用于推导该蛋白质家族中两个11个氨基酸重复序列的共有序列。
The primary and secondary structure of human plasma apolipoprotein A-I and apolipoprotein E-3 have been analyzed to further our understanding of the secondary and tertiary conformation of these proteins and the structure and function of plasma lipoprotein particles. The methods used to analyze the primary sequence of these proteins used computer programs: (a) to identify repeated patterns within these proteins on the basis of conservative substitutions and similarities within the physicochemical properties of each residue; (b) for local averaging, hydrophobic moment, and Fourier analysis of the physicochemical properties; and (c) for secondary structure prediction of each protein carried out using homology, statistical, and information theory based methods. Circular dichroism was used to study purified lipid-protein complexes of each protein and quantitate the secondary structure in a lipid environment. The data from these analyses were integrated into a single secondary structure prediction to derive a model of each protein. The sequence homology within apolipoproteins A-I, E-3, and A-IV is used to derive a consensus sequence for two 11 amino acid repeating sequences in this family of proteins.