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 55
... fraction consists predominantly of pili . ( c ) Bottom . A fraction from the digest shown in ( a ) isolated by chromatography on agarose . This fraction consists pre- dominantly of " doughnuts , " but some short fragments of pili are ...
... fraction consists predominantly of pili . ( c ) Bottom . A fraction from the digest shown in ( a ) isolated by chromatography on agarose . This fraction consists pre- dominantly of " doughnuts , " but some short fragments of pili are ...
Page 385
... Fraction BG is the globulin fraction obtained by ammonium sulfate precipitation of the material withdrawn from the bottom reservoir after the final ( eleventh ) stage of fractionation . See Cann and Loveless ( 1957 ) for details ...
... Fraction BG is the globulin fraction obtained by ammonium sulfate precipitation of the material withdrawn from the bottom reservoir after the final ( eleventh ) stage of fractionation . See Cann and Loveless ( 1957 ) for details ...
Page 386
... fraction to be isolated ( Sorof and Ott , 1954 ) . This density gradient effectively prevents the passage of convective currents originating from the bottom section , thereby allowing electrophoresis of much longer duration than usual ...
... fraction to be isolated ( Sorof and Ott , 1954 ) . This density gradient effectively prevents the passage of convective currents originating from the bottom section , thereby allowing electrophoresis of much longer duration than usual ...
Contents
SLAYTER | 2 |
Basic Techniques in Specimen Preparation for Electron | 10 |
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 conformational changes 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 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 Phys plot polarization polymer produced protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone