Physical biochemistry : principles and applications /
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| Author / Creator: | Sheehan, David, 1958- |
|---|---|
| Edition: | 2nd ed. |
| Imprint: | Chichester, UK ; Hoboken, NJ : Wiley-Blackwell, 2009. |
| Description: | xiv, 407 p., [8] p. of plates : ill. (some col.) ; 26 cm. |
| Language: | English |
| Subject: | |
| Format: | Print Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/7773107 |
Table of Contents:
- Preface
- Acknowledgements
- Chapter 1. Introduction
- 1.1. Special chemical requirements of biomolecules
- 1.2. Factors affecting analyte structure and stability
- 1.2.1. pH effects
- 1.2.2. Temperature effects
- 1.2.3. Effects of solvent polarity
- 1.3. Buffering systems used in biochemistry
- 1.3.1. How does a buffer work?
- 1.3.2. Some common buffers
- 1.3.3. Additional components often used in buffers
- 1.4. Quantitation, units and data handling
- 1.4.1. Units used in this text
- 1.4.2. Quantitation of protein and biological activity
- 1.5. Objectives of this book Bibliography
- Chapter 2. Chromatography
- 2.1. Principles of chromatography
- 2.1.1. The partition coefficient
- 2.1.2. Phase systems used in biochemistry
- 2.1.3. Liquid chromatography
- 2.1.4. Gas chromatography
- 2.2. Performance parameters used in chromatography
- 2.2.1. Retention
- 2.2.2. Resolution
- 2.2.3. Physical basis of peak broadening
- 2.2.4. Plate height equation
- 2.2.5. Capacity factor
- 2.2.5. Peak symmetry
- 2.2.7. Significance of performance criteria in chromatography
- 2.3. Chromatography equipment
- 2.3.1. Outline of standard system used
- 2.3.2. Components of a chromatography system
- 2.3.3. Stationary phases used
- 2.3.4. Elution
- 2.4. Modes of chromatography
- 2.4.1. Ion exchange
- 2.4.2. Gel filtration
- 2.4.3. Reversed phase
- 2.4.4. Hydrophobic interaction
- 2.4.5. Affinity
- 2.4.6. Immobilised metal affinity chromatography
- 2.4.7. Hydroxyapatite
- 2.5. Open-column chromatography
- 2.5.1. Equipment used
- 2.5.2. Industrial-scale chromatography of proteins
- 2.6. High-performance liquid chromatography
- 2.6.1. Equipment used
- 2.6.2. Stationary phases in HPLC
- 2.6.3. Liquid phases in HPLC
- 2.7. Fast protein liquid chromatography
- 2.7.1. Equipment used
- 2.7.2. Comparison with HPLC
- 2.8. Perfusion chromatography
- 2.8.1. Theory of perfusion chromatography
- 2.8.2. The practice of perfusion chromatography
- 2.9. Membrane-based chromatography systems
- 2.9.1. Theoretical basis
- 2.9.2. Applications of membrane-based separations
- 2.10. Chromatography of a sample protein
- 2.10.1. Designing a purification protocol
- 2.10.2. Ion exchange chromatography of a sample protein:Glutathione S-transferases
- 2.10.3. HPLC of peptides from glutathione S-transferases Bibliography
- Chapter 3. Spectroscopic Techniques
- 3.1. The nature of light
- 3.1.1. A brief history of the theories of light
- 3.1.2. Wave-particle duality theory of light
- 3.2. The electromagnetic spectrum
- 3.2.1. The Electromagnetic Spectrum
- 3.2.2. Transitions in spectroscopy
- 3.3. Ultraviolet/visible absorption spectroscopy
- 3.3.1. Physical basis
- 3.3.2. Equipment used in absorption spectroscopy
- 3.3.3. Applications of absorption spectroscopy
- 3.4. Fluorescence spectroscopy
- 3.4.1. Physical basis of fluorescence and related phenomena
- 3.4.2. Measurement of fluorescence and chemiluminescence
- 3.4.3. External quenching of fluorescence
- 3.4.4. Uses of fluorescence in binding studies
- 3.4.5. Protein-folding studies
- 3.4.6. Resonance energy transfer
- 3.4.7. Applications of fluorescence in cell biology
- 3.5. Spectroscopic techniques using plane-polarised light
- 3.5.1. Polarised light
- 3.5.2. Chirality in biomolecules
- 3.5.3. Circular dichroism (CD)
- 3.5.4. Equipment used in CD
- 3.5.5. CD of biopolymers
- 3.5.6. Linear dichroism (LD)
- 3.5.7. LD of biomolecules
- 3.5.8. Plasmon resonance spectroscopy
- 3.6. Infrared spectroscopy
- 3.6.1. Physical basis of infrared spectroscopy
- 3.6.2. Equipment used in infrared spectroscopy
- 3.6.3. Uses of infrared spectroscopy in structure d
