Guan Xiaoyan, Rastogi Neha, Parthun Mark R, Freitas Michael A
Department of Chemistry and Biochemistry, The Ohio State University , 100 West 18th Avenue, Columbus, Ohio 43210, United States.
J Proteome Res. 2014 Feb 7;13(2):506-16. doi: 10.1021/pr400675n. Epub 2014 Jan 9.
This paper describes an algorithm to assist in relative quantitation of peptide post-translational modifications using stable isotope labeling by amino acids in cell culture (SILAC). The described algorithm first determines the normalization factor and then calculates SILAC ratios for a list of target peptide masses using precursor ion abundances. Four yeast histone mutants were used to demonstrate the effectiveness of this approach for quantitation of peptide post-translational modifications changes. The details of the algorithm's approach for normalization and peptide ratio calculation are described. The examples demonstrate the robustness of the approach as well as its utility to rapidly determine changes in peptide post-translational modifications within a protein.
本文描述了一种算法，该算法借助细胞培养中氨基酸稳定同位素标记法（SILAC）协助进行肽段翻译后修饰的相对定量分析。所描述的算法首先确定归一化因子，然后使用前体离子丰度计算一系列目标肽段质量的SILAC比率。使用四个酵母组蛋白突变体来证明该方法在定量肽段翻译后修饰变化方面的有效性。描述了该算法用于归一化和肽段比率计算的方法细节。这些示例证明了该方法的稳健性及其在快速确定蛋白质内肽段翻译后修饰变化方面的实用性。
