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 110
... interactions between oriented chromophore and solvent molecules is called the orientation shift . Two other interactions between chromophores and solvent occur . The first and most ubiquitous is the London dispersion interaction , the ...
... interactions between oriented chromophore and solvent molecules is called the orientation shift . Two other interactions between chromophores and solvent occur . The first and most ubiquitous is the London dispersion interaction , the ...
Page 410
... interaction between proteins and small molecules for situations in which the protein is acid to its iso- electric point ( with positive mobilities and the mobility of the complexed protein molecule being assumed greater than that of the ...
... interaction between proteins and small molecules for situations in which the protein is acid to its iso- electric point ( with positive mobilities and the mobility of the complexed protein molecule being assumed greater than that of the ...
Page 439
... interactions have been pre- sented above for carboxylate , phosphate - borate , borate , and tris - borate buffers . There is also ample evidence for multiple electrophoretic peaks generated by interaction with solvents containing amino ...
... interactions have been pre- sented above for carboxylate , phosphate - borate , borate , and tris - borate buffers . There is also ample evidence for multiple electrophoretic peaks generated by interaction with solvents containing amino ...
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 contrast 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 energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups heavy atom 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