Author ORCID Identifier
Document Type
Article
Publication Date
3-8-2017
Abstract
Protein footprinting mediated by mass spectrometry has evolved over the last 30 years from proof of concept to commonplace biophysics tool, with unique capabilities for assessing structure and dynamics of purified proteins in physiological states in solution. This review outlines the history and current capabilities of two major methods of protein footprinting: reversible hydrogen-deuterium exchange (HDX) and hydroxyl radical footprinting (HRF), an irreversible covalent labeling approach. Technological advances in both approaches now permit high-resolution assessments of protein structure including secondary and tertiary structure stability mediated by backbone interactions (measured via HDX) and solvent accessibility of side chains (measured via HRF). Applications across many academic fields and in biotechnology drug development are illustrated including: detection of protein interfaces, identification of ligand/drug binding sites, and monitoring dynamics of protein conformational changes along with future prospects for advancement of protein footprinting in structural biology and biophysics research.
Publication Title
Molecular & Cellular Proteomics
Volume
16
Issue
5
First Page
706
Last Page
716
Rights
©2017 by The American Society for Biochemistry and Molecular Biology, Inc.
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Liwen Wang, Mark R. Chance. Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment. Molecular & Cellular Proteomics, Volume 16, Issue 5, 2017, Pages 706-716, https://doi.org/10.1074/mcp.O116.064386.