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 160
... buffer ) to each of a series of tightly stoppered vials ( or matched cuvettes , if a sufficient number are available ) . For spectrophotometric titrations , identical aliquots of a series of buffer solutions are then added , one to each ...
... buffer ) to each of a series of tightly stoppered vials ( or matched cuvettes , if a sufficient number are available ) . For spectrophotometric titrations , identical aliquots of a series of buffer solutions are then added , one to each ...
Page 436
... buffer ( pH 6.1 , ionic strength 0.043 ) , or a phosphate - borate buffer of about the same pH and ionic strength . The zone patterns are presented in Figs . 26a and 26b ; whereas the protein gave a single zone in phosphate buffer , two ...
... buffer ( pH 6.1 , ionic strength 0.043 ) , or a phosphate - borate buffer of about the same pH and ionic strength . The zone patterns are presented in Figs . 26a and 26b ; whereas the protein gave a single zone in phosphate buffer , two ...
Page 438
... buffer . Also , human myoglobin gives three zones on starch gel in a tris - borate buffer due to a reaction ( Kossman et al . , 1964 ) , although it is not clear whether it is a protein - buffer inter- action . In all these cases ...
... buffer . Also , human myoglobin gives three zones on starch gel in a tris - borate buffer due to a reaction ( Kossman et al . , 1964 ) , although it is not clear whether it is a protein - buffer inter- action . In all these cases ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
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 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