Physical Principles and Techniques of Protein Chemistry, Part 1Sydney J. Leach Physical Principles and Techniques of Protein Chemistry, Part A deals with the principles and application of selected physical methods in protein chemistry evaluation. This book is organized into nine chapters that cover microscopic, crystallographic, and electrophoretic techniques for protein conformational perturbations evaluation. This text first presents a general account of electron microscopy, its specimen preparation, optimum conditions for high resolution, measurement of electron micrographs, and illustrative examples of protein study. This book then examines the different types of map ... |
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Page 386
... complex mixtures is often hampered by the occurrence of convection in the electrophoresis cell . When the more rapidly descend- ing boundaries migrate into the bottom section of the cell , convection due to gravitational instability ...
... complex mixtures is often hampered by the occurrence of convection in the electrophoresis cell . When the more rapidly descend- ing boundaries migrate into the bottom section of the cell , convection due to gravitational instability ...
Page 418
... complex and , in fact , its area proved to be an empirical index of the extent of binding of serum albumin by pepsin . " Several independent lines of evidence were presented suggesting that this complex is the spe- cific Michaelis ...
... complex and , in fact , its area proved to be an empirical index of the extent of binding of serum albumin by pepsin . " Several independent lines of evidence were presented suggesting that this complex is the spe- cific Michaelis ...
Page 419
... complex between a proteolytic enzyme and its macromolecular substrate . Previously , the existence of the Michaelis- Menten complex had been shown only for low molecular weight sub- strates ( Chance , 1943 , 1951 ; Doherty and Vaslow ...
... complex between a proteolytic enzyme and its macromolecular substrate . Previously , the existence of the Michaelis- Menten complex had been shown only for low molecular weight sub- strates ( Chance , 1943 , 1951 ; Doherty and Vaslow ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Copyright | |
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absorption absorption spectrum amino acids applied axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration conformational changes contrast curve Debye denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ionization ions light macromolecules measured method migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic Phys plot polarization polymer produced protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone