Protein-ligand interactions : methods and applications
- نوع فایل : کتاب
- زبان : انگلیسی
- مؤلف : G Ulrich Nienhaus
- ناشر : Totowa, N.J. : Humana Press
- چاپ و سال / کشور: 2005
- شابک / ISBN : 9781588293725
Description
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: harnessing multivalent protein-surface interactions for purification procedures -- 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 -- 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: resonance raman spectroscopy as a probe of functional intermediates -- Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: effects of errors and uncertainties -- Ligand binding with stopped-flow rapid mixing -- Circular dichroism spectroscopy for the study of protein-ligand interactions -- High throughput screening of interactions between G protein-coupled 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: challenges and applications -- Force probe molecular dynamics simulations -- Study of ligand-protein interactions by means of density functional theory and first-principles molecular dynamics
