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 127
... carboxyl and a - amino groups . The change in absorption for each dis- sociation step depends upon the wavelength . From Fig . 10 , A € 292 for titration of both the carboxyl and amino groups is positive ( low pH reference solution ) ...
... carboxyl and a - amino groups . The change in absorption for each dis- sociation step depends upon the wavelength . From Fig . 10 , A € 292 for titration of both the carboxyl and amino groups is positive ( low pH reference solution ) ...
Page 128
... carboxyl Tryptophan Indole Carboxyl 293 240 0.053 2.8 Tryptophan Indole Amino 295 680 0.150 Glycyltryptophan Indole Carboxyl 294 270 0.059 Glycyltryptophan Indole Amino 294 68 0.015 Histidine Imidazole Carboxyl 226.5 300 0.053 2.7 ...
... carboxyl Tryptophan Indole Carboxyl 293 240 0.053 2.8 Tryptophan Indole Amino 295 680 0.150 Glycyltryptophan Indole Carboxyl 294 270 0.059 Glycyltryptophan Indole Amino 294 68 0.015 Histidine Imidazole Carboxyl 226.5 300 0.053 2.7 ...
Page 129
... carboxyl group in acetyl - glycine and glycyl- glycine more than doubles the absorption of the amide group at 205 mμ , as shown by the spectrophotometric titrations of Fig . 11 . B. SOLVENT PERTURBATION The immediate environment of a ...
... carboxyl group in acetyl - glycine and glycyl- glycine more than doubles the absorption of the amide group at 205 mμ , as shown by the spectrophotometric titrations of Fig . 11 . B. SOLVENT PERTURBATION The immediate environment of a ...
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