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 ... |
From inside the book
Results 1-3 of 29
Page 2
... shape of particles , of changes in shape , and of morphological features of molecular interactions . Quantitative measurements may also be made from electron micrographs . At the present time , the resolving power of electron ...
... shape of particles , of changes in shape , and of morphological features of molecular interactions . Quantitative measurements may also be made from electron micrographs . At the present time , the resolving power of electron ...
Page 182
... shape for the pro- tein or a random orientation of the fluorescent label with respect to the coordinate axes of the protein . 2. The molecule is completely rigid , with no internal degrees of rota- tional freedom . 3. The shape of the ...
... shape for the pro- tein or a random orientation of the fluorescent label with respect to the coordinate axes of the protein . 2. The molecule is completely rigid , with no internal degrees of rota- tional freedom . 3. The shape of the ...
Page 358
... shape of the buildup curve that the orientation is due primarily to an induced polarization . The same conclusion was also reached from the frequency dependence of the birefringence in al- ternating fields of 20 to 20,000 cycles / sec ...
... shape of the buildup curve that the orientation is due primarily to an induced polarization . The same conclusion was also reached from the frequency dependence of the birefringence in al- ternating fields of 20 to 20,000 cycles / sec ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
45 other sections not shown
Other editions - View all
Common terms and phrases
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