Ion Mobility-Mass Spectrometry to Evaluate the Effects of Protein Modification or Small Molecule Binding on Protein Dynamics

Tomlinson, Lauren J and Eyers, Claire E ORCID: 0000-0002-3223-5926 (2020) Ion Mobility-Mass Spectrometry to Evaluate the Effects of Protein Modification or Small Molecule Binding on Protein Dynamics. ION MOBILITY-MASS SPECTROMETRY: METHODS AND PROTOCOLS, 2084. pp. 179-190. ISSN 1064-3745, 1940-6029

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Abstract

Ion mobility-mass spectrometry (IM-MS) of intact protein complexes under native conditions is a powerful tool for the analysis of protein complexes and protein-ligand interactions, permitting insight into ligand-induced changes in protein conformation. Here we describe a procedure for analyzing the effects of phosphorylation and/or inhibitor binding on protein kinase conformational flexibility using Protein Kinase A (PKA) as a model system. By calculating the protein collision cross section (CCS) before and after inhibitor binding, and additionally by performing collision-induced unfolding (CIU), we can establish the effects of protein modification or small molecule binding on protein dynamics.

Item Type:	Article
Uncontrolled Keywords:	Ion mobility-mass spectrometry, Native mass spectrometry, Collision cross section, Collision-induced unfolding
Depositing User:	Symplectic Admin
Date Deposited:	02 Dec 2019 09:43
Last Modified:	07 Dec 2024 18:53
DOI:	10.1007/978-1-0716-0030-6_11
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3064395