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Mass Spectrometry in Structural Biology: Surface‐induced Dissociation/Ion Mobility of Protein Complexes
Author(s) -
Wysocki Vicki,
Quintyn Royston,
Harvey Sophie,
Song Yang,
Yan Jing,
Ju Yue,
Tanimoto Akiko,
Sahasrabuddhe Aniruddha
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.360.3
Subject(s) - mass spectrometry , protein subunit , dissociation (chemistry) , chemistry , structural biology , ion mobility spectrometry , topology (electrical circuits) , stoichiometry , protein structure , biophysics , crystallography , chemical physics , biochemistry , biology , chromatography , mathematics , combinatorics , gene
Characterization of the overall topology and inter‐subunit contacts of protein complexes, and their assembly/disassembly and unfolding pathways, is critical because protein complexes regulate key biological processes, including processes important in understanding and controlling disease. Conventional structural biology methods such as X‐ray crystallography and nuclear magnetic resonance provide high‐resolution information on the structures of protein complexes and are the gold standards in the field. However, other emerging biophysical methods that only provide lower resolution data (e.g. stoichiometry and subunit connectivity) on the structures of the protein complexes are also important. Native mass spectrometry is one of these approaches that provide lower resolution, but critical, structural information with high throughput. The power of native MS increases when coupled to ion mobility (IM‐MS), a technique that measures rotationally averaged collisional cross sections and thus direct information on conformational changes. This presentation illustrates a new approach, surface‐induced dissociation/ion mobility (SID/IM) MS, for characterization of topology, intersubunit connectivity, and other structural features (degree of unfolding) of multimeric protein complexes.