Characterization of Complete Histone Tail Proteoforms Using Differential Ion Mobility Spectrometry

Overview

Journal Anal Chem

Specialty Chemistry

Date 2017 Apr 14

PMID 28406606

Citations 11

Authors

Pavel V Shliaha

Matthew A Baird

Mogens M Nielsen

Vladimir Gorshkov

Andrew P Bowman

Julia L Kaszycki

Ole N Jensen

Alexandre A Shvartsburg

Affiliations

Soon will be listed here.

Abstract

Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all functional PTMs are found on the N-terminal histone domains (tails) of ∼50 residues protruding from the nucleosome core. Using high-definition differential ion mobility spectrometry (FAIMS) with electron transfer dissociation, we demonstrate rapid baseline gas-phase separation and identification of tails involving monomethylation, trimethylation, acetylation, or phosphorylation in biologically relevant positions. These are by far the largest variant peptides resolved by any method, some with PTM contributing just 0.25% to the mass. This opens the door to similar separations for intact proteins and in top-down proteomics.

Citing Articles

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