Biophysical Chemistry of Proteins
An Introduction to Laboratory Methods
(Sprache: Englisch)
This comprehensive and clearly structured text begins with an overview of analytical techniques and moves on to discuss the full range of relevant issues, from purification of proteins and their modification to enzyme kinetics and laboratory quality control.
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This comprehensive and clearly structured text begins with an overview of analytical techniques and moves on to discuss the full range of relevant issues, from purification of proteins and their modification to enzyme kinetics and laboratory quality control.
Klappentext zu „Biophysical Chemistry of Proteins “
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.
Inhaltsverzeichnis zu „Biophysical Chemistry of Proteins “
Part One: Analytical techniques1. 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
Autoren-Porträt von Engelbert Buxbaum
Dr. Buxbaum's research interests are enzymology and protein structure/function relationship. In addition, he has been teaching science and medical students in several countries. He is currently working as associate professor of biochemistry at Ross University School of Medicine.
Bibliographische Angaben
- Autor: Engelbert Buxbaum
- 2014, 2011, XVI, 510 Seiten, Masse: 15,6 x 23,6 cm, Kartoniert (TB), Englisch
- Verlag: Springer, Berlin
- ISBN-10: 1489982132
- ISBN-13: 9781489982131
Sprache:
Englisch
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