Author ORCID Identifier

Mark R. Chance

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

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

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COinS
10.1074/mcp.O116.064386" data-hide-no-mentions="true">
10.1074/mcp.O116.064386" data-hide-zero-citations="true" data-style="small_circle">
 
 

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