Protein Interactions

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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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.

• Sedimentation
• Titration
• fluorescence
• microscopy
• protein complexes
• proteins
• proteins, protein interaction, schuck

• National Institutes of Health, Bethesda, USA

  Peter Schuck

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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