Which technique is used to analyze posttranslational modification of proteins such as histone acetylation?

The technique most suitable for analyzing posttranslational modifications of proteins, such as histone acetylation, is mass spectrometry. This method allows for the identification and quantification of protein modifications at a molecular level, enabling researchers to determine the presence and specific sites of modifications, such as acetylation on histones.

Mass spectrometry is particularly powerful because it can analyze complex mixtures of proteins and their modifications, providing detailed information about molecular weights, sequences, and the types of chemical changes that have occurred. This is crucial for understanding the dynamic regulation of histone acetylation and its role in gene expression and chromatin structure.

While methods like Western blotting can detect specific proteins and posttranslational modifications when specific antibodies are available, they do not provide the comprehensive analytical capacity of mass spectrometry. Similarly, gel electrophoresis can separate proteins based on size but does not directly identify or characterize modifications. RNA sequencing focuses on transcriptome analysis and would not apply to protein modifications.