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Chemical cross‐linking and native mass spectrometry: A fruitful combination for structural biology
Author(s) -
Sinz Andrea,
Arlt Christian,
Chorev Dror,
Sharon Michal
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2696
Subject(s) - structural biology , mass spectrometry , computational biology , protein–protein interaction , chemical biology , chemistry , protein structure , protein chemistry , biophysics , nanotechnology , biology , biological system , biochemistry , materials science , chromatography
Mass spectrometry (MS) is becoming increasingly popular in the field of structural biology for analyzing protein three‐dimensional‐structures and for mapping protein–protein interactions. In this review, the specific contributions of chemical crosslinking and native MS are outlined to reveal the structural features of proteins and protein assemblies. Both strategies are illustrated based on the examples of the tetrameric tumor suppressor protein p53 and multisubunit vinculin‐Arp2/3 hybrid complexes. We describe the distinct advantages and limitations of each technique and highlight synergistic effects when both techniques are combined. Integrating both methods is especially useful for characterizing large protein assemblies and for capturing transient interactions. We also point out the future directions we foresee for a combination of in vivo crosslinking and native MS for structural investigation of intact protein assemblies.