Protein interactions : biophysical approaches for the study of complex reversible systems
Author(s)
Bibliographic Information
Protein interactions : biophysical approaches for the study of complex reversible systems
（Protein reviews, v. 5）
Springer, c2007
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Includes bibliographical references and index
Description and Table of Contents
Description
This volume successfully and clearly examines how biophysical approaches can be used to study complex systems of reversibly interacting proteins. It deals with the methodology behind the research and shows how to synergistically incorporate several methodologies for use. Each chapter treats and introduces the reader to different biological systems, includes a brief summary of the physical principles, and mentions practical requirements.
Table of Contents
The Characterization of Biomolecular Interactions Using Fluorescence Fluctuation Techniques.- Characterization of Protein-Protein Interactions Using Atomic Force Microscopy.- Combined Solid-Phase Detection Techniques for Dissecting Multiprotein Interactions on Membranes.- Surface Plasmon Resonance Biosensing in the Study of Ternary Systems of Interacting Proteins.- Mass Spectrometry for Studying Protein Modifications and for Discovery of Protein Interactions.- H/2H Exchange Mass Spectrometry of Protein Complexes.- Elucidation of Protein-Protein and Protein-Ligand Interactions by NMR Spectroscopy.- Application of Isothermal Titration Calorimetry in Exploring the Extended Interface.- Solvent Mediated Protein-Protein Interactions.- Sedimentation Equilibrium Analytical Ultracentrifugation for Multicomponent Protein Interactions.- Structure Analysis of Macromolecular Complexes by Solution Small-Angle Scattering.- Fluorescence Detection of Proximity.- Steady-State and Time-Resolved Emission Anisotropy.- Analysis of Protein-DNA Equilibria by Native Gel Electrophoresis.- Electrospray Ionization Mass Spectrometry and the Study of Protein Complexes.- Sedimentation Velocity in the Study of Reversible Multiprotein Complexes.
by "Nielsen BookData"
