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 249
... equilibrium position characterized by a higher ( usually by 5 ° -10 ° C ) temperature . Similarly , the ... equilibrium . Since the equilibrium constant for this reaction is assumed to be temperature dependent , the equilibrium ...
... equilibrium position characterized by a higher ( usually by 5 ° -10 ° C ) temperature . Similarly , the ... equilibrium . Since the equilibrium constant for this reaction is assumed to be temperature dependent , the equilibrium ...
Page 482
... equilibrium . However , the gel filtration data on aryl sulfatase A ( Fig . 7 ) serve to emphasize that the difference may only reflect the magnitude of the association constant in relation to the pro- tein concentration used for ...
... equilibrium . However , the gel filtration data on aryl sulfatase A ( Fig . 7 ) serve to emphasize that the difference may only reflect the magnitude of the association constant in relation to the pro- tein concentration used for ...
Page 492
... equilibrium concentrations of B directly for this combination of elution volumes ( Vo = VA < VB ) . Thus , although ... equilibrium concentra- tion of B is obtained directly from the trailing profile for systems con- forming with this ...
... equilibrium concentrations of B directly for this combination of elution volumes ( Vo = VA < VB ) . Thus , although ... equilibrium concentra- tion of B is obtained directly from the trailing profile for systems con- forming with this ...
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