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      Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment.

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          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.

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          Author and article information

          Journal
          Mol. Cell Proteomics
          Molecular & cellular proteomics : MCP
          American Society for Biochemistry & Molecular Biology (ASBMB)
          1535-9484
          1535-9476
          May 2017
          : 16
          : 5
          Affiliations
          [1 ] From the ‡Center for Proteomics and Bioinformatics, Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio.
          [2 ] From the ‡Center for Proteomics and Bioinformatics, Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio mark.chance@case.edu.
          Article
          O116.064386
          10.1074/mcp.O116.064386
          5417815
          28275051
          71826da3-55b6-4957-a3d8-d87ef2d2a97a
          History

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