Del 305 - Methods in Molecular Biology

Protein'Ligand Interactions

Methods and Applications

Inbunden, Engelska, 2005

Av G. Ulrich Nienhaus, G. Ulrich Nienhaus

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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™ 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.

Produktinformation

Utgivningsdatum2005-03-21
Mått155 x 235 x 41 mm
Vikt1 140 g
FormatInbunden
SpråkEngelska
SerieMethods in Molecular Biology
Antal sidor568
Upplaga2005
FörlagHumana Press Inc.
ISBN9781588293725

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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.