G. Ulrich Nienhaus (ed.)

Protein'Ligand Interactions

Methods and Applications
Herausgegeben:Nienhaus, G. Ulrich

• Gebundenes Buch

Produktbeschreibung

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.

Produktdetails

• Methods in Molecular Biology 305
• Verlag: Humana / Humana Press / Springer, Berlin
• Artikelnr. des Verlages: 978-1-58829-372-5
• 2005
• Seitenzahl: 584
• Erscheinungstermin: 21. März 2005
• Englisch
• Abmessung: 241mm x 160mm x 41mm
• Gewicht: 2g
• ISBN-13: 9781588293725
• ISBN-10: 1588293726
• Artikelnr.: 20992833

Inhaltsangabe

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.