Quantifying homologous proteins and proteoforms release_hwajjkgflbea5o36eitfungh2q

by Dmitry Malioutov, Tianchi Chen, Jacob Jaffe, Edoardo Airoldi, Steven Carr, Bogdan Budnik, Nikolai Slavov

Released as a report .

2017  

Abstract

Many proteoforms - arising from alternative splicing, post-translational modifications (PTMs), or paralogous genes - have distinct biological functions, such as histone PTM proteoforms. However, their quantification by existing bottom-up mass-spectrometry (MS) methods is undermined by peptide-specific biases. To avoid these biases, we developed and implemented a first-principles model (HIquant) for quantifying proteoform stoichiometries. We characterized when MS data allow inferring proteoform stoichiometries by HIquant, derived an algorithm for optimal inference, and demonstrated experimentally high accuracy in quantifying fractional PTM occupancy without using external standards, even in the challenging case of the histone modification code. HIquant server is implemented at: https://web.northeastern.edu/slavov/2014_HIquant/
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Type  report
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Date   2017-08-05
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Language   en ?
Number  mcp.TIR118.000947
arXiv  1708.01772v1
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