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 132
... glycol " 1.433115 4.4 0.072 110 0.047 270 ° Glycerol 1.473525 5.2 0.060 90 Dimethylsulfoxide 1.478721 4.0 0.158 240 0.087 484 / Polyethylene glycol 9.2 0.135 200 Sucrose 9.4 0.040 60 a From Herskovits and Laskowski ( 1962a , b ) for N ...
... glycol " 1.433115 4.4 0.072 110 0.047 270 ° Glycerol 1.473525 5.2 0.060 90 Dimethylsulfoxide 1.478721 4.0 0.158 240 0.087 484 / Polyethylene glycol 9.2 0.135 200 Sucrose 9.4 0.040 60 a From Herskovits and Laskowski ( 1962a , b ) for N ...
Page 141
... glycol chitin , which does not absorb in the ultraviolet , produces a red shift in the absorption of an indole chromophore when it is added to lysozyme solutions ( Hayashi et al . , 1963 ) . The difference spectrum , Fig . 16 , is ...
... glycol chitin , which does not absorb in the ultraviolet , produces a red shift in the absorption of an indole chromophore when it is added to lysozyme solutions ( Hayashi et al . , 1963 ) . The difference spectrum , Fig . 16 , is ...
Page 222
... glycol ( Weber , 1960b ) . The excitation polarization spectrum of tryptophan is more complex than that of tyrosine since it exhibits two maxima ( at 267-270 and 300-305 mμ ) and two minima ( at 290 and 232 mμ ) ( Weber , 1960a ) . The ...
... glycol ( Weber , 1960b ) . The excitation polarization spectrum of tryptophan is more complex than that of tyrosine since it exhibits two maxima ( at 267-270 and 300-305 mμ ) and two minima ( at 290 and 232 mμ ) ( Weber , 1960a ) . The ...
Contents
SLAYTER | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum amino acids applied axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration contrast curve Debye denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis electrophoretic patterns elution volume emission energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups heavy atom intensity interactions ionic strength ionization ions light macromolecules measured method 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 protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shadow shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone