Biophysical Chemistry of Proteins

Analytical techniques.- Microscopy.- Single molecule techniques.- Preparation of cells and tissues for microscopy.- Principles of optical spectroscopy.- Photometry.- Fluorimetry.- Chemiluminescence.- Electrophoresis.- Immunological methods.- Isotope techniques.- Purification of proteins.- Homogenisation and fractionisation of cells and tissues.- Isolation of organelles.- Precipitation methods.- Chromatography.- Membrane proteins.- Determination of protein concentration.- Cell culture.- Protein modification and inactivation.- General technical remarks.- Amine-reactive reagents.- Thiol- and disulphide reactive reagents.- Reagents for other groups.- Cross-linkers.- Detection methods.- Spontaneous reactions in proteins.- Protein size and shape.- Centrifugation.- Osmotic pressure.- Diffusion.- Viscosity.- Non-resonant interactions with electromagnetic waves.- Protein structure.- Protein sequencing.- Synthesis of peptides.- Protein secondary structure.- Structure of protein-ligand complexes.- 3D-structures.- Folding and unfolding of proteins.- Enzyme kinetics.- Steady-state kinetics.- Leaving the steady state: Analysis of progress curves.- Reaction velocities.- Isotope effects.- Isotope exchange.- Protein-ligand interactions.- General conditions for interpretable results.- Binding equations.- Methods to measure binding equilibria.- Temperature effects on binding equilibrium and reaction rate.- Industrial enzymology.- Industrial enzyme use.- Immobilised enzymes.- Special statistics.- Quality control.- Testing whether or not a model fits the data.- Appendix.- List of symbols.- Greek alphabet.- Properties of electrophoretic buffers.- Bond properties.- Acronyms.