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 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 | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorbance absorption change absorption spectrum amino acids angle axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Chem chromophores coefficient concentration conformational changes contrast curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effect electric birefringence electric field electron microscope electrophoresis elution emission energy equation equilibrium excitation experimental factor film fluorescence frequency function gel filtration glycol instrument intensity interactions ionic strength ionization ions light macromolecules measured method mobility molar molecular weight molecules moving-boundary observed obtained optical parameter particles patterns peaks permanent dipole phase phenolic phenolic groups phenylalanine photomultiplier Phys polarization produced protein proton quantum yield ratio reaction relaxation residues ribonuclease rotational diffusion sample scattering shift shown in Fig solution solvent specimen spectra spectrofluorometer structure technique temperature theory tion tryptophan tyrosine ultraviolet unit cell values wavelength Weber zone