Read more
A readily reproducible collection of established and emerging techniques for studying the interaction between proteins and ligands, including biochemical/bulk techniques, structure analysis, spectroscopy, single-molecule studies, and theoretical/computational tools. Among the highlights are surface plasmon resonance (SPR) and reflectometric biosensor approaches, high-throughput screening with confocal optics microscopy, single molecule fluorescence and fluorescence correlation spectroscopy (FCS), atomic force microscopy (AFM), crystallography of reaction intermediates, and time-resolved x-ray crystallography. The protocols follow the successful Methods in Molecular Biology(TM) series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
List of contents
Isothermal Titration Calorimetry.- Direct Optical Detection of Protein-Ligand Interactions.- Label-Free Detection of Protein-Ligand Interactions by the Quartz Crystal Microbalance.- Measurement of Solvent Accessibility at Protein-Protein Interfaces.- Hydrophobic Interaction Chromatography.- Sedimentation Velocity Method in the Analytical Ultracentrifuge for the Study of Protein-Protein Interactions.- Protein-Ligand Interaction Probed by Time-Resolved Crystallography.- X-Ray Crystallography of Protein-Ligand Interactions.- Combined Use of XAFS and Crystallography for Studying Protein-Ligand Interactions in Metalloproteins.- NMR Studies of Protein-Ligand Interactions.- Probing Heme Protein-Ligand Interactions by UV/Visible Absorption Spectroscopy.- Ultrafast Time-Resolved IR Studies of Protein-Ligand Interactions.- Monitoring Protein-Ligand Interactions by Time-Resolved FTIR Difference Spectroscopy.- Proteins in Motion.- Fluorescence Polarization/Anisotropy Approaches to Study Protein-Ligand Interactions.- Ligand Binding With Stopped-Flow Rapid Mixing.- Circular Dichroism Spectroscopy for the Study of Protein-Ligand Interactions.- High-Throughput Screening of Interactions Between G ProteinCoupled Receptors and Ligands Using Confocal Optics Microscopy.- Single-Molecule Study of Protein-Protein and Protein-DNA Interaction Dynamics.- Application of Fluorescence Correlation Spectroscopy to Hapten-Antibody Binding.- Atomic Force Microscopy Measurements of Protein-Ligand Interactions on Living Cells.- Computer Simulation of Protein-Ligand Interactions.- Force Probe Molecular Dynamics Simulations.- Study of Ligand-Protein Interactions by Means of Density Functional Theory and First-Principles Molecular Dynamics.
Summary
A readily reproducible collection of established and emerging techniques for studying the interaction between proteins and ligands, including biochemical/bulk techniques, structure analysis, spectroscopy, single-molecule studies, and theoretical/computational tools. Among the highlights are surface plasmon resonance (SPR) and reflectometric biosensor approaches, high-throughput screening with confocal optics microscopy, single molecule fluorescence and fluorescence correlation spectroscopy (FCS), atomic force microscopy (AFM), crystallography of reaction intermediates, and time-resolved x-ray crystallography.
