Mass spectrometry as a tool for protein structure analysis

Petr Pompach, Pavla Vaòková

Institute of Biotechnology v.v.i., Czech Academy of Sciences

petr.pompach@ibt.cas.cz

 

Structural mass spectrometry (MS3D) is a fast-growing field of analytical chemistry that provides an impressive array of structural information about protein topology, conformational dynamics and protein-protein/ligand interaction. To gain this kind of information, well-established techniques are used in CMS, encompassing hydrogen-deuterium exchange (HDX), chemical cross-linking and native mass spectrometry. Importantly, all of these techniques are compatible with membrane proteins. The structural mass spectrometry core facility is equipped with state-of-the-art instrumentation such as 15T FT-ICR, timsToF SCP, timsToF Pro, automation system for HDX and UPLC or nanoUPLC systems. Beyond MS3D, the core facility offers other MS-based proteomic approaches providing protein identification, quantification, precise intact protein molecular mass determination, and characterization of various protein posttranslational modifications (phosphorylation, glycosylation, acetylation, biotinylation, etc.), or disulfide bond linkages assignment. The inherent advantages of these MS-based approaches are their sensitivity, low sample consumption and complementarity to other biophysical techniques.

CIISB, Instruct-CZ Centre of Instruct-ERIC EU consortium, funded by MEYS CR infrastructure project LM2023042 and European Regional Development Fund-Project „UP CIISB“ (No. CZ.02.1.01/0.0/0.0/18_046/0015974), is gratefully acknowledged for the financial support of the Structural mass spectrometry core facility.