Biophysical Chemistry of Proteins

Part One: Analytical techniques1.Microscopy2.Single molecule techniques3.Preparation of cells and tissues for microscopy4.Principles of optical spectroscopy5.Photometry6.Fluorimetry7.Chemiluminescence8.Electrophoresis9.Immunological methods10.Isotope techniquesPart Two: Purification of proteins11.Homogenisation and fractionisation of cells and tissues12.Isolation of organelles13.Precipitation methods14.Chromatography15.Membrane proteins16.Determination of protein concentration17.Cell culturePart Three: Protein modification and inactivation18.General technical remarks19.Amine-reactive reagents20.Thiol- and disulphide reactive reagents21.Reagents for other groups22.Cross-linkers23.Detection methods24.Spontaneous reactions in proteinsPart Four: Protein size and shape25.Centrifugation26.Osmotic pressure27.Diffusion28.Viscosity29.Non-resonant interactions with electromagnetic wavesPart Five: Protein structure30.Protein sequencing31.Synthesis of peptides32.Protein secondary structure33.Structure of protein-ligand complexes34.3D-structures35.Folding and unfolding of proteinsPart Six: Enzyme kinetics36.Steady-state kinetics37.Leaving the steady state: Analysis of progress curves38.Reaction velocities39.Isotope effects40.Isotope exchangePart Seven: Protein-ligand interactions41.General conditions for interpretable results42.Binding equations43.Methods to measure binding equilibria44.Temperature effects on binding equilibrium and reaction ratePart Eight: Industrial enzymology45.Industrial enzyme use46.Immobilised enzymesPart Nine: Special statistics47.Quality control48.Testing whether or not a model fits the dataPart Ten: Appendix49.List of symbols50.Greek alphabet51.Properties of electrophoretic buffers52.Bond properties53.Acronyms... Mehr