Protein'Ligand Interactions

1. Front Matter

   Pages i-xi

   PDF

2. Isothermal Titration Calorimetry

   • Edwin A. Lewis, Kenneth P. Murphy

   Pages 1-15

3. Direct Optical Detection of Protein-Ligand Interactions

   • Frank Gesellchen, Bastian Zimmermann, Friedrich W. Herberg

   Pages 17-45

4. Label-Free Detection of Protein-Ligand Interactions by the Quartz Crystal Microbalance

   • Andreas Janshoff, Claudia Steinem

   Pages 47-63

5. Measurement of Solvent Accessibility at Protein-Protein Interfaces

   • Jeffrey G. Mandell, Abel Baerga-Ortiz, Arnold M. Falick, Elizabeth A. Komives

   Pages 65-79

6. Hydrophobic Interaction Chromatography

   • Herbert P. Jennissen

   Pages 81-99

7. Sedimentation Velocity Method in the Analytical Ultracentrifuge for the Study of Protein-Protein Interactions

   • Claus Urbanke, Gregor Witte, Ute Curth

   Pages 101-113

8. Protein-Ligand Interaction Probed by Time-Resolved Crystallography

   • Marius Schmidt, Hyotcherl Ihee, Reinhard Pahl, Vukica Šrajer

   Pages 115-154

9. X-Ray Crystallography of Protein-Ligand Interactions

   • Ilme Schlichting

   Pages 155-165

10. Combined Use of XAFS and Crystallography for Studying Protein-Ligand Interactions in Metalloproteins

    • Richard W. Strange, S. Samar Hasnain

    Pages 167-196

11. NMR Studies of Protein-Ligand Interactions

    • Till Maurer

    Pages 197-213

12. Probing Heme Protein-Ligand Interactions by UV/Visible Absorption Spectroscopy

    • Karin Nienhaus, G. Ulrich Nienhaus

    Pages 215-241

13. Ultrafast Time-Resolved IR Studies of Protein-Ligand Interactions

    • Manho Lim, Philip A. Anfinrud

    Pages 243-259

14. Monitoring Protein-Ligand Interactions by Time-Resolved FTIR Difference Spectroscopy

    • Carsten Kötting, Klaus Gerwert

    Pages 261-285

15. Proteins in Motion

    • Uri Samuni, Joel M. Friedman

    Pages 287-300

16. Fluorescence Polarization/Anisotropy Approaches to Study Protein-Ligand Interactions

    • David M. Jameson, Gabor Mocz

    Pages 301-322

17. Ligand Binding With Stopped-Flow Rapid Mixing

    • Mark S. Hargrove

    Pages 323-341

18. Circular Dichroism Spectroscopy for the Study of Protein-Ligand Interactions

    • Alison Rodger, Rachel Marrington, David Roper, Stuart Windsor

    Pages 343-363

19. High-Throughput Screening of Interactions Between G ProteinCoupled Receptors and Ligands Using Confocal Optics Microscopy

    • Lenka Zemanová, Andreas Schenk, Martin J. Valler, G. Ulrich Nienhaus, Ralf Heilker

    Pages 365-383

20. Single-Molecule Study of Protein-Protein and Protein-DNA Interaction Dynamics

    • H. Peter Lu

    Pages 385-413

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.

• biology
• biosensors
• microscopy
• molecular biology
• protein
• proteins
• receptor

• Department of Biophysics, University of Ulm, Ulm, Germany

  G. Ulrich Nienhaus

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