Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics

Chance, M.

1. Edition October 2008
304 Pages, Hardcover
Practical Approach Book

ISBN: 978-0-470-25886-6

John Wiley & Sons

Short Description

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.

A how-to guide that helps you take advantage of the latest mass spectrometry methods

This book brings together and examines the latest mass spectrometry methods used to investigate proteins, including structural mechanisms, protein dynamics, and interactions among proteins. Written by a team of experts with many years of hands-on experience developing and working with mass spectrometry methods, the book offers a wealth of practical advice and tips to help readers fully exploit the capabilities of a mass spectrometer.

The book begins with an overview of mass spectrometry technologies, including an expert forecast of future directions. Next, the authors offer step-by-step guidance for such topics as:
* Complementary methods for structure determination: hydroxyl radical-mediated footprinting and deuterium exchange mass spectrometry as applied to serpin structure
* Covalent labeling methods for examining protein structure and protein interactions
* Computational approaches to examine protein-protein interactions: combining experimental and computational data in the era of structural genomics
* Two approaches to mass spectrometric protein footprinting: PLIMSTEX and FPOP
* Hydrogen/deuterium exchange studies of viruses

Carefully edited, the book presents a uniform standard of high quality and thoroughness throughout all the chapters. References to the literature enable readers to explore each individual topic in greater depth.

Any researcher seeking to advance his or her own protein research will benefit from this book's insights and how-to guidance. The spectrometry methods can be applied to support investigations in such fields as biomedicine, biotechnology, and pharmaceutical research.

Foreword.

Contributors.

1. Overview of Mass Spectrometry Technologies for Examining Protein Structure: Current and Future Directions (Shannon M. Swiatkowski and Mark R. Chance).

References.

2. Hydrogen Exchange Mass Spectrometry: Principles and Capabilities (Sebastien Brier and John R. Engen).

Acknowledgment.

References.

3. Covalent Labeling Methods for Examining Protein Structure and Protein Interactions (Keiji Takamoto and Janna Kiselar).

References.

4. Complementary Methods for Structure Determination: Hydroxyl-Radical-Mediated Footprinting and Deuterium Exchange Mass Spectrometry as Applied to Serpin Structure (Xiaojing Zheng and Patrick L. Wintrode).

Acknowledgement.

References.

5. Deuterium Exchange Approaches for Examining Protein Interactions: Case Studies of Complex Formation (Elizabeth A. Komives).

References.

6. Hydrogen/Deuterium Exchange Studies of Viruses (Sebyung Kang and Peter E. Prevelige Jr.).

References.

7. Use of Enhanced Peptide Amide Hydrogen/Deuterium Exchange-Mass Spectrometry (DXMS) in the Examination of Protein-Protein Interactions (Yoshitomo Hamuro, Stephen J. Coales, Lora L. Hamuro, and Virgil L. Woods Jr.).

Abbreviations.

Acknowledgements.

References.

8. Cross-linking as a Tool to Examine Protein Complexes: Examples of Cross-linking Strategies and Computational Modeling (Evgeniy V. Petrotchenko and Christoph H. Borchers).

References.

9. Complex Formation in the Actin Cytoskeleton: Cross-linking Tools to Define Actin Protein Structure and Interactions (Sabrina Benchaar and Emil Reisler).

Acknowledgement.

References.

10. Computational Approaches to Examining Protein-Protein Interactions: Combining Experimental and Computational Data in the Era of Structural Genomics (J.K. Amisha Kamal).

Acknowledgment.

References.

11. Studies of Intact Proteins and Protein Complexes: ESI MS Approaches (Igor A. Kaltashov, Rinat R. Abzalimov, Agya K. Frimpong, and Stephen J. Eyles).

Acknowledgments.

References.

12. Two Approaches to Mass Spectrometric Protein Footprinting: PLIMSTEX and FPOP (Michael L. Gross, Mei M. Zhu, and David M. Hambly).

Abbreviations.

Acknowledgments.

References.

Index.

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.