Enhanced descriptions from Syndetics:

An accessible and easy-to-read text for students requiring a broad overview of the key techniques used to characterise the structure and function of complex biomacromolecules such as proteins and DNA. It bridges the gap between general biochemistry textbooks and the more specialist texts covering individual techniques.
Topics covered include chromatography, spectroscopy, mass spectrometry, electrophoresis, X-ray diffraction, centrifugation and biocalorimetry. New developments are placed in context by describing the physical principles on which they depend, examining the range of biophysical applications most widely used and, emphasising the overall similarities of experimental approach.
Written by a biochemist with extensive teaching experience, the book:
* describes the advantages and disadvantages of each technique and compares one technique to another;
* introduces experimental approaches in a non-mathematical way, using practical examples; and
* provides a bibliography, including useful web sites, at the end of each chapter.
This book will be invaluable to undergraduates and postgraduates studying biochemistry, molecular biology and related disciplines.

Table of contents provided by Syndetics

• 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