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 142
... BONDS IN PROTEINS Many discussions of difference spectra of proteins have been concerned with the problem of ... bond will not ordinarily be detected . A discussion of the energy levels of the ionized and un - ionized phenolic ...
... BONDS IN PROTEINS Many discussions of difference spectra of proteins have been concerned with the problem of ... bond will not ordinarily be detected . A discussion of the energy levels of the ionized and un - ionized phenolic ...
Page 147
... bond is cleaved by action of the enzyme ( Finkenstadt and Laskowski , 1965 ) . Changes produced upon peptide bond hydrolysis during activation of chymotrypsinogen ( Cher- venka , 1959 ) appear to be an example of the second type . The ...
... bond is cleaved by action of the enzyme ( Finkenstadt and Laskowski , 1965 ) . Changes produced upon peptide bond hydrolysis during activation of chymotrypsinogen ( Cher- venka , 1959 ) appear to be an example of the second type . The ...
Page 226
... bonds involved in a conformational change can approach the two limiting possibilities of either participation of all the bonds , as in the highly cooperative helix - coil transition , or of rupture of only a single bond . The ability to ...
... bonds involved in a conformational change can approach the two limiting possibilities of either participation of all the bonds , as in the highly cooperative helix - coil transition , or of rupture of only a single bond . The ability to ...
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