Biophysical chemistry of proteins : an introduction to laboratory methods
Author(s)
Bibliographic Information
Biophysical chemistry of proteins : an introduction to laboratory methods
Springer Science+Business Media, c2011
Available at 3 libraries
  Aomori
  Iwate
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University Library for Agricultural and Life Sciences, The University of Tokyo図
464.2:B975010634003
Note
Bibliographical references: p. 465-486
Includes index
Description and Table of Contents
Description
The book is structured in nine sections, each containing several chapters. The volume starts with an overview of analytical techniques and progresses through purification of proteins; protein modification and inactivation; protein size, shape, and structure; enzyme kinetics; protein-ligand interactions; industrial enzymology; and laboratory quality control. The book is targeted at all scientists interested in protein research.
Table of Contents
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
by "Nielsen BookData"