Quantitative analysis of isotope distributions in proteomic mass spectrometry using least-squares Fourier transform convolution
Quantitative analysis of isotope distributions in proteomic mass spectrometry using least-squares Fourier transform convolution
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DOI：
10.1021/ac800080v
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发表时间：
2008-07-01
影响因子：
7.4
通讯作者：
Williamson, James R.
中科院分区：
文献类型：
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作者：
Sperling, Edit;Bunner, Anne E.;Williamson, James R.
定量蛋白质组学质谱法涉及由不同同位素标记模式产生的峰的幅度的比较，所述同位素标记模式包括分数原子标记和分数残基标记。我们已经开发了一个通用的和灵活的分析处理的复杂的同位素分布，出现在这些实验中，使用，傅立叶变换卷积计算标记的同位素分布和最小二乘法定量比较与实验峰。分数原子和分数残基标记的程度可以从实验峰确定，同时作为同位素分布中所有同位素异构体的积分强度。使用分数N-15-标记和分数C-13-异亮氨酸标记的数据来说明该方法。最小二乘傅里叶变换卷积方法可以应用于许多类型的定量蛋白质组学数据，包括细胞培养和脉冲标记实验中的氨基酸稳定同位素标记的数据。
Quantitative proteomic mass spectrometry involves comparison of the amplitudes of peaks resulting from different isotope labeling patterns, including fractional atomic labeling and fractional residue labeling. We have developed a general and flexible analytical treatment of the complex isotope distributions that arise in these experiments, using, Fourier transform convolution to calculate labeled isotope distributions and least-squares for quantitative comparison with experimental peaks. The degree of fractional atomic and fractional residue labeling can be determined from experimental peaks at the same time as the integrated intensity of all of the isotopomers in the isotope distribution. The approach is illustrated using data with fractional N-15-labeling and fractional C-13-isoleucine labeling. The least-squares Fourier transform convolution approach can be applied to many types of quantitive proteomic data, including data from stable isotope labeling by amino acids in cell culture and pulse labeling experiments.