With proteomics entering the third decade, the identification and quantification of primary protein sequences has become a mature science. Many analytical challenges remain during the mapping of post-translational modifications (PTMs) of proteins, especially in their native state. For example, complete deciphering of the "histone code" entails the identification and localization of the different PTMs using top-down strategies. While some advances have been made, traditional LC-MS/MS methods cannot fully separate histones with isomeric PTM position variants; this leads to the need to further develop new, fast, and orthogonal separations that can be easily integrated with mass spectrometry for the characterization of the “histone code”. In the present talk, we will describe the advantages of coupling trapped ion mobility spectrometry and top-down tandem mass spectrometry. Examples will be shown of the implementation of non-ergodic fragmentation using electron (ExD) based and photon (UVPD) based top-down approaches for the characterization of histone tails and histone proteoforms.

Characterization of histone proteoforms using TIMS-{ExD, UVPD}-MS/MS

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.