Protein'Ligand Interactions
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Protein'Ligand Interactions : Methods and Applications

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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 (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.
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Product details

  • Hardback | 568 pages
  • 157.5 x 231.1 x 35.6mm | 1,088.63g
  • Humana Press Inc.
  • Totowa, NJ, United States
  • English
  • 2005 ed.
  • XI, 568 p.
  • 1588293726
  • 9781588293725

Back cover copy

Molecular recognition and binding of ligands (atoms, ions, and molecules) by proteins with high sensitivity and selectivity is of central importance to essentially all biomolecular processes and of key importance for the basic and applied sciences. In Protein-Ligand Interactions: Methods and Applications, leading experts with hands-on experience describe in detail a broad selection of established and emerging techniques for studying the interaction between proteins and ligands, including bulk biochemical 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.
Cutting-edge and highly practical, Protein-Ligand Interactions: Methods and Applications offers novice and expert researchers alike a broad selection of powerful and widely applicable techniques that can be used to efficiently and successfully solve the task of characterizing protein-ligand interactions.
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Table of contents

Isothermal Titration Calorimetry
Edwin A. Lewis and Kenneth P. Murphy

Direct Optical Detection of Protein-Ligand Interactions
Frank Gesellchen, Bastian Zimmermann, and Friedrich W. Herberg

Label-Free Detection of Protein-Ligand Interactions by the Quartz Crystal Microbalance
Andreas Janshoff and Claudia Steinem

Measurement of Solvent Accessibility at Protein-Protein Interfaces
Jeffrey G. Mandell, Abel Baerga-Ortiz, Arnold M. Falick, and Elizabeth A. Komives

Hydrophobic Interaction Chromatography: Harnessing Multivalent Protein-Surface Interactions for Purification Procedures
Herbert P. Jennissen

Sedimentation Velocity Method in the Analytical Ultracentrifuge for the Study of Protein-Protein Interactions
Claus Urbanke, Gregor Witte, and Ute Curth

Protein-Ligand Interaction Probed by Time-Resolved Crystallography
Marius Schmidt, Hyotcherl Ihee, Reinhard Pahl, and Vukica Srajer

X-Ray Crystallography of Protein-Ligand Interactions
Ilme Schlichting

Combined Use of XAFS and Crystallography for Studying Protein-Ligand Interactions in Metalloproteins
Richard W. Strange and S. Samar Hasnain

NMR Studies of Protein-Ligand Interactions
Till Maurer

Probing Heme Protein-Ligand Interactions by UV/Visible Absorption Spectroscopy
Karin Nienhaus and G. Ulrich Nienhaus

Ultrafast Time-Resolved IR Studies of Protein-Ligand Interactions
Manho Lim and Philip A. Anfinrud

Monitoring Protein-Ligand Interactions by Time-Resolved FTIR Difference Spectroscopy
Carsten Koetting and Klaus Gerwert

Proteins in Motion: Resonance Raman Spectroscopy as a Probe of Functional Intermediates
Uri Samuni and Joel M. Friedman

Fluorescence Polarization/Anisotropy Approaches to Study Protein-Ligand Interactions: Effects of Errors and Uncertainties
David M. Jameson and GaborMocz

Ligand Binding With Stopped-Flow Rapid Mixing
Mark S. Hargrove

Circular Dichroism Spectroscopy for the Study of Protein-Ligand Interactions
Alison Rodger, Rachel Marrington, David Roper, and Stuart Windsor

High-Throughput Screening of Interactions Between G Protein-Coupled Receptors and Ligands Using Confocal Optics Microscopy
Lenka Zemanova, Andreas Schenk, Martin J. Valler, G. Ulrich Nienhaus, and Ralf Heilker

Single-Molecule Study of Protein-Protein and Protein-DNA Interaction Dynamics
H. Peter Lu

Application of Fluorescence Correlation Spectroscopy to Hapten-Antibody Binding
Theodore L. Hazlett, Qiaoqiao Ruan, and Sergey Y. Tetin

Atomic Force Microscopy Measurements of Protein-Ligand Interactions on Living Cells
Robert H. Eibl and Vincent T. Moy

Computer Simulation of Protein-Ligand Interactions: Challenges and Applications
Sergio A. Hassan, Luis Gracia, Geetha Vasudevan, and Peter J. Steinbach

Force Probe Molecular Dynamics Simulations
Helmut Grubmuller

Study of Ligand-Protein Interactions by Means of Density Functional Theory and First-Principles Molecular Dynamics
Carme Rovira

Index
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