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 43
... region of the specimen in the vicinity of that sphere . Other parts of the specimen might differ significantly in their distance from the shadowing source , and the effective shadow ratio for those regions would differ accordingly ...
... region of the specimen in the vicinity of that sphere . Other parts of the specimen might differ significantly in their distance from the shadowing source , and the effective shadow ratio for those regions would differ accordingly ...
Page 202
... region than in another , and in in- struments like the Aminco - Bowman spectrofluorometer , the emission grating is maximally efficient at 500 mμ ( Howerton , 1959 ) . The grating , like the phototube , is interchangeable , and by ...
... region than in another , and in in- struments like the Aminco - Bowman spectrofluorometer , the emission grating is maximally efficient at 500 mμ ( Howerton , 1959 ) . The grating , like the phototube , is interchangeable , and by ...
Page 361
... regions of 4.0 to 5.0 and 7.0 to 9.0 . A permanent dipole moment along the transverse axis was found in the low pH region ; the ... region . The observed data were interpreted in terms of 7. DIELECTRIC PROPERTIES OF PROTEINS II 361.
... regions of 4.0 to 5.0 and 7.0 to 9.0 . A permanent dipole moment along the transverse axis was found in the low pH region ; the ... region . The observed data were interpreted in terms of 7. DIELECTRIC PROPERTIES OF PROTEINS II 361.
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