An Introduction to Laboratory Methods
Buch, Englisch, 510 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 951 g
ISBN: 978-1-4419-7250-7
Verlag: Springer US
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.
Zielgruppe
Graduate
Autoren/Hrsg.
Fachgebiete
- Naturwissenschaften Biowissenschaften Zellbiologie
- Naturwissenschaften Biowissenschaften Angewandte Biologie Biophysik
- Naturwissenschaften Biowissenschaften Proteinforschung
- Naturwissenschaften Physik Angewandte Physik Biophysik
- Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Medizin, Gesundheitswesen Biomedizin, Medizinische Forschung, Klinische Studien
- Naturwissenschaften Chemie Organische Chemie Biochemie
- Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
Weitere Infos & Material
Analytical techniques. Microscopy. Single molecule techniques. Preparation of cells and tissues for microscopy. Principles of optical spectroscopy.Photometry. Fluorimetry. Chemiluminescence.Electrophoresis.Immunological methods.Isotope techniques.- Purification of proteins.Homogenisation and fractionisation of cells and tissues.Isolation of organelles. Precipitation methods.Chromatography. Membrane proteins. Determination of protein concentration.Cell culture.- Protein modification and inactivation. General technical remarks. Amine-reactive reagents. Thiol- and disulphide reactive reagents. Reagents for other groups. Cross-linkers.Detection methods. Spontaneous reactions in proteins.- Protein size and shape. Centrifugation.Osmotic pressure. Diffusion.Viscosity.Non-resonant interactions with electromagnetic waves.- Protein structure. Protein sequencing.Synthesis of peptides. Protein secondary structure. Structure of protein-ligand complexes. 3D-structures. Folding and unfolding of proteins.- Enzyme kinetics. Steady-state kinetics. Leaving the steady state: Analysis of progress curves.Reaction velocities. Isotope effects. Isotope exchange.- Protein-ligand interactions. General conditions for interpretable results. Binding equations.Methods to measure binding equilibria. Temperature effects on binding equilibrium and reaction rate.- Industrial enzymology. Industrial enzyme use.Immobilised enzymes.- Special statistics.Quality control. Testing whether or not a model fits the data.- Appendix. List of symbols.Greek alphabet. Properties of electrophoretic buffers. Bond properties. Acronyms.