Hiding behind hydrophobicity -: Transmembrane segments in mass spectrometry
Hiding behind hydrophobicity -: Transmembrane segments in mass spectrometry
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DOI：
10.1074/jbc.m405875200
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发表时间：
2004-12-03
影响因子：
4.8
通讯作者：
Schleiff, E
中科院分区：
文献类型：
--
作者：
Eichacker, LA;Granvogl, B;Schleiff, E
膜蛋白的蛋白质组学对于理解细胞功能是必不可少的。然而，膜蛋白质组的质谱分析不如可溶性蛋白质组学测定成功。为了阐明跨膜蛋白质在质谱中的奥秘，我们提出了一个详细的统计分析来自叶绿体膜的实验数据。该方法进一步通过计算机消化后的拟南芥蛋白质组分析来完成。我们表明，长度和疏水性的蛋白水解片段含有跨膜段是主要的决定因素，通过质谱检测。基于比较分析，我们讨论了克服这个问题的可能性，并提供了可能的协议，转移的疏水性跨膜段的肽，以促进其检测。
Proteomics of membrane proteins is essential for the understanding of cellular function. However, mass spectrometric analysis of membrane proteomes has been less successful than the proteomic determination of soluble proteins. To elucidate the mystery of transmembrane proteins in mass spectrometry, we present a detailed statistical analysis of experimental data derived from chloroplast membranes. This approach was further accomplished by the analysis of the Arabidopsis thaliana proteome after in silico digestion. We demonstrate that both the length and the hydrophobicity of the proteolytic fragments containing transmembrane segments are major determinants for detection by mass spectrometry. Based on a comparative analysis, we discuss possibilities to overcome the problem and provide possible protocols to shift the hydrophobicity of transmembrane segment-containing peptides to facilitate their detection.