Physicochemical factors for discriminating between soluble and membrane proteins: hydrophobicity of helical segments and protein length
Physicochemical factors for discriminating between soluble and membrane proteins: hydrophobicity of helical segments and protein length
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DOI：
10.1093/protein/12.11.953
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发表时间：
1999-11-01
期刊：
影响因子：
--
通讯作者：
Hirokawa, T
中科院分区：
文献类型：
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作者：
Mitaku, S;Hirokawa, T
多肽片段的平均疏水性被认为是跨膜螺旋形成中最重要的因素，将最疏水（MH）片段分配到替代的非极性环境中，球状蛋白的膜或疏水核心可能决定产生的蛋白质类型，为了阐明MH片段在确定给定氨基酸序列产生两种类型蛋白质中的哪一种方面的重要性，我们统计研究了长于19个残基的Mn螺旋的特征长度方面，包括 97 种三维结构或拓扑已知的膜蛋白，以及从蛋白质数据库中选出的 397 种可溶性蛋白。膜蛋白中Mn螺旋的平均疏水性与蛋白质的长度具有特征性关系。膜蛋白中长度超过 500 个残基的所有 Mn 螺旋的疏水性都大于 1.75（Kyte 和 Doolittle 标度），而膜蛋白中小于 100 个残基的 MH 螺旋的亲水性可能高达 0.1。讨论了开发一种根据大小对产生的蛋白质类型的影响来区分膜蛋白和可溶性蛋白的方法的可能性。
The average hydrophobicity of a polypeptide segment is considered to be the most important factor in the formation of transmembrane helices, and the partitioning of the most hydrophobic (MH) segment into the alternative nonpolar environment, a membrane or hydrophobic core of a globular protein may determine the type of protein produced, In order to elucidate the importance of the MH segment in determining which of the two types of protein results from a given amino acid sequence, we statistically studied the characteristics of Mn helices, longer than 19 residues in length, in 97 membrane proteins whose three-dimensional structure or topology is known, as well as 397 soluble proteins selected from the Protein Data Bank. The average hydrophobicity of Mn helices in membrane proteins had a characteristic relationship with the length of the protein. All Mn helices in membrane proteins that were longer than 500 residues had a hydrophobicity greater than 1.75 (Kyte and Doolittle scale), while the MH helices in membrane proteins smaller than 100 residues could be as hydrophilic as 0.1. The possibility of developing a method to discriminate membrane proteins from soluble ones, based on the effect of size on the type of protein produced, is discussed.