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Protein Interactions

Biophysical Approaches for the Study of Complex Reversible Systems

  • Book
  • © 2007

Overview

Editors:
  1. Peter Schuck

    1. National Institutes of Health, Bethesda, USA

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  • Examines how biophysical approaches can be used to study complex systems of reversibly interacting proteins and shows how to synergistically incorporate several methodologies for use
  • Covers calorimetry, fluorescence, surface plasmon resonance, evanescent wave biosensors, mass spectroscopy, electrophoretic mobility, FRET, H-D exchange methods, solvent-mediated protein interactions, and other methodologies
  • Explores interacting protein partners, binding protein, protein modifications, protein analysis, complex protein systems, and other protein interactions
  • Is part of the Protein Reviews series
  • Includes supplementary material: sn.pub/extras

Part of the book series: Protein Reviews (PRON, volume 5)

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Table of contents (16 chapters)

  1. Front Matter

    Pages i-xi
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  2. The Characterization of Biomolecular Interactions Using Fluorescence Fluctuation Techniques

    • Emmanuel Margeat, Hacène Boukari, Catherine A. Royer
    Pages 1-38

  3. Characterization of Protein–Protein Interactions Using Atomic Force Microscopy

    • Hong Wang, Yong Yang, Dorothy A. Erie
    Pages 39-77

  4. Combined Solid-Phase Detection Techniques for Dissecting Multiprotein Interactions on Membranes

    • Jacob Piehler
    Pages 79-96

  5. Surface Plasmon Resonance Biosensing in the Study of Ternary Systems of Interacting Proteins

    • Eric J. Sundberg, Peter S. Andersen, Inna I. Gorshkova, Peter Schuck
    Pages 97-141

  6. Mass Spectrometry for Studying Protein Modifications and for Discovery of Protein Interactions

    • Peter S. Backlund Jr., Alfred L. Yergey
    Pages 143-167

  7. H/2H Exchange Mass Spectrometry of Protein Complexes

    • Elizabeth A. Komives
    Pages 169-187

  8. Elucidation of Protein–Protein and Protein–Ligand Interactions by NMR Spectroscopy

    • Hans Robert Kalbitzer, Werner Kremer, Frank Schumann, Michael Spörner, Wolfram Gronwald
    Pages 189-229

  9. Application of Isothermal Titration Calorimetry in Exploring the Extended Interface

    • John E. Ladbury, Mark A. Williams
    Pages 231-254

  10. Solvent Mediated Protein–Protein Interactions

    • Christine Ebel
    Pages 255-287

  11. Sedimentation Equilibrium Analytical Ultracentrifugation for Multicomponent Protein Interactions

    • Peter Schuck
    Pages 289-316

  12. Structure Analysis of Macromolecular Complexes by Solution Small-Angle Scattering

    • D. I. Svergun, P. Vachette
    Pages 317-365

  13. Fluorescence Detection of Proximity

    • K. Wojtuszewski, J. J. Harvey, M. K. Han, J. R. Knutson
    Pages 367-396

  14. Steady-State and Time-Resolved Emission Anisotropy

    • K. Wojtuszewski, J. R. Knutson
    Pages 397-416

  15. Analysis of Protein-DNA Equilibria by Native Gel Electrophoresis

    • Claire A. Adams, Michael G. Fried
    Pages 417-446

  16. Electrospray Ionization Mass Spectrometry and the Study of Protein Complexes

    • Alan M. Sandercock, Carol V. Robinson
    Pages 447-468

  17. Sedimentation Velocity in the Study of Reversible Multiprotein Complexes

    • Peter Schuck
    Pages 469-518

  18. Back Matter

    Pages 519-532
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Keywords

About this book

When I was invited to edit this volume, I wanted to take the opportunity to assemble reviews of different biophysical methodologies for protein interactions at a level suf?ciently detailed to understand how complex systems can be studied. There are several excellent introductory texts for biophysical methodologies, many with hands-on descriptions or embedded in general introductions to physical b- chemistry. The goal of the present volume was to present state-of-the-art reviews that do not necessarily enable the reader to carry out these techniques, but to gain a deep understanding of the biophysical observables, to stimulate creative thought on how the techniques may be applied to study a particular biological system, and to foster collaboration and multidisciplinary work. Reversible protein interactions involve noncovalent chemical bonds, pro- cing protein complexes with free energies not far from the order of magnitude of the thermal energy kT. As a consequence, they can be highly dynamic and may be controlled, for example, by protein expression levels and changes in the intracel- lar or microenvironment. Reversible protein complexes may have suf?cient stab- ity to be puri?ed for study, but frequently their short lifetime essentially limits their existence to solutions of mixtures of the binding partners in which they remain populated through dissociation and reassociation processes. To understand the function of such protein complexes, it is important to study their structure and dynamics.

Editors and Affiliations

  • National Institutes of Health, Bethesda, USA

    Peter Schuck

About the editor

Dr. Peter Schuck is the acting chief of the Protein Biophysics department in the National Institute of Health’s Division of Bioengineering and Physical Science. His current research work is on protein structure and function, with studies in multi-protein complexes, membrane proteins in detergent solution, self-assembling and filamenting proteins, structural and nonstructural viral proteins, homogeneous and heterogeneous interactions of immunological cell surface receptors; and biophysical methods and instrumentation through analytical ultracentrifugation, optical biosensors, static and dynamic light scattering, calorimetry, and circular dichroism.

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