Analysis of protein–drug interactions by ion mobility–mass spectrometry (CAT#: STEM-ST-0145-LJX)

Introduction

An important consideration during drug development is the structural and mechanistic evaluation of the protein target, ideally combined with a multi-level understanding of how conformation and biological function are modulated by ligand binding. Ion mobility–mass spectrometry (IM–MS), which separates ions in the gas-phase based on their size (mass), shape and charge has emerged as an important addition to more traditional structural biology techniques such as NMR, X-ray crystallography and Cryo-electron microscopy [8] and can be readily exploited to help understand conformational dynamics of proteins and non-covalent protein complexes.