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 37
... method of course depends upon a choice of pH and composition of the contrasting medium which is compatible with the stability of the specimen . C. EMBEDDING The methods of fixation , embedding , and ultrathin sectioning used in the ...
... method of course depends upon a choice of pH and composition of the contrasting medium which is compatible with the stability of the specimen . C. EMBEDDING The methods of fixation , embedding , and ultrathin sectioning used in the ...
Page 85
... method of isomorphous replacement . This method requires the preparation of crystals of one or more heavy atom derivatives of the protein in which the unit cell dimen- sions , the molecular conformation , and the position and ...
... method of isomorphous replacement . This method requires the preparation of crystals of one or more heavy atom derivatives of the protein in which the unit cell dimen- sions , the molecular conformation , and the position and ...
Page 279
... methods are simple , accurate , and capable of a high resolution , but they require large volumes of reactant solutions ( often 0.5-1 liter ) . 2. The Stopped - Flow Method This technique is by far the more important of the flow methods ...
... methods are simple , accurate , and capable of a high resolution , but they require large volumes of reactant solutions ( often 0.5-1 liter ) . 2. The Stopped - Flow Method This technique is by far the more important of the flow methods ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration curve 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 enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ions lens light linear macromolecules measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone