Biophysical Chemistry of Proteins
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Biophysical Chemistry of Proteins

An Introduction to Laboratory Methods
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Engelbert Buxbaum
951 g
241x160x33 mm

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.
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.
Focuses on the biophysical chemistry of proteinsPresents an overview of the methods used in protein research
Examines the possible applications and limitations of protein research
Part One: Analytical techniques1.Microscopy2.Single molecule techniques3.Preparation of cells and tissues for microscopy4.Principles of optical spectroscopy5.Photometry6.Fluorimetry7.Chemiluminescence8.Electrophoresis9.Immunological methods10.Isotope techniquesPart Two: Purification of proteins11.Homogenisation and fractionisation of cells and tissues12.Isolation of organelles13.Precipitation methods14.Chromatography15.Membrane proteins16.Determination of protein concentration17.Cell culturePart Three: Protein modification and inactivation18.General technical remarks19.Amine-reactive reagents20.Thiol- and disulphide reactive reagents21.Reagents for other groups22.Cross-linkers23.Detection methods24.Spontaneous reactions in proteinsPart Four: Protein size and shape25.Centrifugation26.Osmotic pressure27.Diffusion28.Viscosity29.Non-resonant interactions with electromagnetic wavesPart Five: Protein structure30.Protein sequencing31.Synthesis of peptides32.Protein secondary structure33.Structure of protein-ligand complexes34.3D-structures35.Folding and unfolding of proteinsPart Six: Enzyme kinetics36.Steady-state kinetics37.Leaving the steady state: Analysis of progress curves38.Reaction velocities39.Isotope effects40.Isotope exchangePart Seven: Protein-ligand interactions41.General conditions for interpretable results42.Binding equations43.Methods to measure binding equilibria44.Temperature effects on binding equilibrium and reaction ratePart Eight: Industrial enzymology45.Industrial enzyme use46.Immobilised enzymesPart Nine: Special statistics47.Quality control48.Testing whether or not a model fits the dataPart Ten: Appendix49.List of symbols50.Greek alphabet51.Properties of electrophoretic buffers52.Bond properties53.Acronyms