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 375
... ionic atmosphere . As a consequence of the electrostatic force between the charge on the particle and the ions of ... strength of the solvent medium . Thus , other things remaining constant , the electrophoretic mobility is expected to ...
... ionic atmosphere . As a consequence of the electrostatic force between the charge on the particle and the ions of ... strength of the solvent medium . Thus , other things remaining constant , the electrophoretic mobility is expected to ...
Page 391
... ionic strength 0.1 ) and a total protein concentration of 2.67 % . He found overall changes in conductance of the order of 6-12 % . Larger changes are to be expected at lower ionic strengths . The author has observed very large changes ...
... ionic strength 0.1 ) and a total protein concentration of 2.67 % . He found overall changes in conductance of the order of 6-12 % . Larger changes are to be expected at lower ionic strengths . The author has observed very large changes ...
Page 396
... ionic strength . Even though a macromole- cule migrates as a single boundary at a single pH and ionic strength , it may still be a mixture of several components which happen to have similar mobilities under the chosen experimental ...
... ionic strength . Even though a macromole- cule migrates as a single boundary at a single pH and ionic strength , it may still be a mixture of several components which happen to have similar mobilities under the chosen experimental ...
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