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Integrating mass spectrometry of intact protein complexes into structural proteomics
Author(s) -
Hyung SukJoon,
Ruotolo Brandon T.
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100520
Subject(s) - proteomics , context (archaeology) , mass spectrometry , chemistry , posttranslational modification , computational biology , ion mobility spectrometry , biochemical engineering , computer science , nanotechnology , data science , biochemistry , chromatography , biology , materials science , engineering , paleontology , gene , enzyme
MS analysis of intact protein complexes has emerged as an established technology for assessing the composition and connectivity within dynamic, heterogeneous multiprotein complexes at low concentrations and in the context of mixtures. As this technology continues to move forward, one of the main challenges is to integrate the information content of such intact protein complex measurements with other MS approaches in structural biology. Methods such as H / D exchange, oxidative foot‐printing, chemical cross‐linking, affinity purification, and ion mobility separation add complementary information that allows access to every level of protein structure and organization. Here, we survey the structural information that can be retrieved by such experiments, demonstrate the applicability of integrative MS approaches in structural proteomics, and look to the future to explore upcoming innovations in this rapidly advancing area.