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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

T-wave ion mobility-mass spectrometry: basic experimental procedures for protein complex analysis.

Izhak Michaelevski¹, Noam Kirshenbaum, Michal Sharon

¹Department of Biological Chemistry, Weizmann Institute of Science.

Journal of Visualized Experiments : Jove

|August 24, 2010

Summary

This summary is machine-generated.

Ion mobility mass spectrometry (IM-MS) separates ions by size and shape, providing structural insights into protein complexes. This method enhances spectral resolution and defines subunit packing under near-physiological conditions.

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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

Analyzing Large Protein Complexes by Structural Mass Spectrometry

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Published on: June 19, 2010

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Area of Science:

Analytical Chemistry
Biochemistry
Structural Biology

Background:

Ion mobility (IM) separates ions based on their collision cross-section (Omega) in a gas phase.
Traveling-wave ion mobility mass spectrometry (T-wave IM-MS) integrates IM with mass spectrometry for 3D data (m/z, intensity, drift time).
This technique reduces spectral overlap and resolves complexes with similar masses but different shapes.

Purpose of the Study:

To provide a detailed protocol for ion mobility mass spectrometry (IM-MS) analysis of protein complexes.
To describe optimization, calibration, data processing, and interpretation methods for IM-MS.
To introduce practical aspects of IM-MS for researchers studying protein assemblies.

Main Methods:

Utilizing a Synapt (Quadrupole-Ion Mobility-Time-of-Flight) HDMS instrument for IM-MS analysis.
Calibrating collision cross-sections using proteins with known structures.
Implementing methods for data processing and calculation of theoretical Omega values.

Main Results:

IM-MS provides an additional dimension of separation, yielding a three-dimensional spectrum.
Drift time measurements offer structural information related to ion shape and topology.
Protein quaternary structure is maintained in the gas phase, enabling the study of protein assemblies.

Conclusions:

IM-MS is a powerful technique for defining the shape and subunit packing of protein assemblies.
The method allows characterization at micromolar concentrations and near-physiological conditions.
This protocol serves as an introduction to practical IM-MS for characterizing protein complexes.