Biophysical Chemistry of Proteins

Part One: Analytical techniques
1. Microscopy
2. Single molecule techniques
3. Preparation of cells and tissues for microscopy
4. Principles of optical spectroscopy
5. Photometry
6. Fluorimetry
7. Chemiluminescence
8. Electrophoresis
9. Immunological methods
10. Isotope techniques

Part Two: Purification of proteins
11. Homogenisation and fractionisation of cells and tissues
12. Isolation of organelles
13. Precipitation methods
14. Chromatography
15. Membrane proteins
16. Determination of protein concentration
17. Cell culture

Part Three: Protein modification and inactivation
18. General technical remarks
19. Amine-reactive reagents
20. Thiol- and disulphide reactive reagents
21. Reagents for other groups
22. Cross-linkers
23. Detection methods
24. Spontaneous reactions in proteins

Part Four: Protein size and shape
25. Centrifugation
26. Osmotic pressure
27. Diffusion
28. Viscosity
29. Non-resonant interactions with electromagnetic waves

Part Five: Protein structure
30. Protein sequencing
31. Synthesis of peptides
32. Protein secondary structure
33. Structure of protein-ligand complexes
34. 3D-structures
35. Folding and unfolding of proteins

Part Six: Enzyme kinetics
36. Steady-state kinetics
37. Leaving the steady state: Analysis of progress curves
38. Reaction velocities
39. Isotope effects
40. Isotope exchange

Part Seven: Protein-ligand interactions
41. General conditions for interpretable results
42. Binding equations
43. Methods to measure binding equilibria
44. Temperature effects on binding equilibrium and reaction rate

Part Eight: Industrial enzymology
45. Industrial enzyme use
46. Immobilised enzymes

Part Nine: Special statistics
47. Quality control
48. Testing whether or not a model fits the data

Part Ten: Appendix
49. List of symbols
50. Greek alphabet
51. Properties of electrophoretic buffers
52. Bond properties
53. Acronyms