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 24
... usually employed as a wire of 0.002 inch diameter ) . However , metals are often evaporated by means of resistance heating , from a refractory fila- ment usually made of tungsten , and in this case the form of the support- ing filament ...
... usually employed as a wire of 0.002 inch diameter ) . However , metals are often evaporated by means of resistance heating , from a refractory fila- ment usually made of tungsten , and in this case the form of the support- ing filament ...
Page 278
... usually possible to obtain a satisfactory result . The practical range of application is 7 - values from about 10-4 μsec to about 10-10 μsec . Since proteins so far have not been studied by cyclic perturbation ( although polyamino acids ...
... usually possible to obtain a satisfactory result . The practical range of application is 7 - values from about 10-4 μsec to about 10-10 μsec . Since proteins so far have not been studied by cyclic perturbation ( although polyamino acids ...
Page 296
... Usually the dielectric constant is a scalar quantity but for anisotropic substances , it is a tensor quantity . C. POLARIZABILITY The magnitude of the dipole moment ; induced by the external field is proportional to the field intensity ...
... Usually the dielectric constant is a scalar quantity but for anisotropic substances , it is a tensor quantity . C. POLARIZABILITY The magnitude of the dipole moment ; induced by the external field is proportional to the field intensity ...
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