Mass Spectrometry Analysis for

This reference presents a wide variety of mass spectrometry methods used to explore structural mechanisms, protein dynamics and interactions between proteins. Preliminary chapters cover mass spectrometry methods for examining proteins and are then followed by chapters devoted to presenting very practical, how-to methods in a detailed way. Methods include deuterium exchange, covalent labeling, footprinting, plistex, and computational approaches. The coverage of footprinting and plistex sets the book apart from the competition.

Mark Chance, PhD, is the Director of the Case Center for Proteomics and Professor of Physiology and Biophysics at Case Western Reserve University. He also directs the Case Center for Synchrotron Biosciences, located at the National Synchrotron Light Source at Brookhaven National Laboratory, New York. Dr. Chance received his bachelor's degree in biology from Wesleyan University and his PhD in biophysics from the University of Pennsylvania. He furthered his training as a postdoctoral research associate at AT&T Bell Laboratories, then went on to become assistant professor in the department of chemistry at Georgetown University. He moved to Albert Einstein College of Medicine in the Bronx, New York, in 1992, and was soon promoted to associate professor of the departments of physiology & biophysics and biochemistry, and full professor in 1998. While at AECOM, he was the Joseph and Anne Wunsch fellow in biophysical engineering and recipient of the Irma Hirschl Career Scientist Award. In 2005, he moved to Case Western Reserve University as the founding director of the Center for Proteomics. His research primarily concerns development of structural and cellular proteomics technologies to understand protein structure-function.

Foreword
Contributors
Overview of Mass Spectrometry Technologies for Examining Protein Structure: Current and Future Directions
Hydrogen Exchange Mass Spectrometry: Principles and Capabilities
Covalent Labeling Methods for Examining Protein Structure and Protein Interactions
Complementary Methods for Structure Determination: Hydroxyl-Radical-Mediated Footprinting and Deuterium Exchange Mass Spectrometry as Applied to Serpin Structure
Deuterium Exchange Approaches for Examining Protein Interactions: Case Studies of Complex Formation
Hydrogen/Deuterium Exchange Studies of Viruses
Use of Enhanced Peptide Amide Hydrogen/Deuterium Exchange-Mass Spectrometry (DXMS) in the Examination of Protein-Protein Interactions
Cross-linking as a Tool to Examine Protein Complexes: Examples of Cross-linking Strategies and Computational Modeling
Complex Formation in the Actin Cytoskeleton: Cross-linking Tools to Define Actin Protein Structure and Interactions
Computational Approaches to Examining Protein-Protein Interactions: Combining Experimental and Computational Data in the Era of Structural Genomics
Studies of Intact Proteins and Protein Complexes: ESI MS Approaches
Two Approaches to Mass Spectrometric Protein Footprinting: PLIMSTEX and FPOP
Index
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Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics

Summary

Author Biography

Table of Contents

Supplemental Materials