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 63
... cell in three dimensions as shown in Fig . 2. The unit cell is characterized by the lengths a , b , and c of its edges and the angles Z α ୪ FIG . 2. A crystal may be regarded as being built up by the three - dimensional repetition of a ...
... cell in three dimensions as shown in Fig . 2. The unit cell is characterized by the lengths a , b , and c of its edges and the angles Z α ୪ FIG . 2. A crystal may be regarded as being built up by the three - dimensional repetition of a ...
Page 162
... cells . In the sample cell , the protein and per- turbant are together . In the reference cell , the protein and perturbant are separated . The amount of water solvent , perturbant , and protein is the same in both beams . The ...
... cells . In the sample cell , the protein and per- turbant are together . In the reference cell , the protein and perturbant are separated . The amount of water solvent , perturbant , and protein is the same in both beams . The ...
Page 163
... cell . Two such cells are prepared like the R1R2 cell in Fig . 25 , with equal volumes of protein separated from equal volumes of perturbant by the vertical partition , and a difference spectrum baseline determined . If the perturbant ...
... cell . Two such cells are prepared like the R1R2 cell in Fig . 25 , with equal volumes of protein separated from equal volumes of perturbant by the vertical partition , and a difference spectrum baseline determined . If the perturbant ...
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