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 61
... single atom of say carbon , we would find that the scattered intensity close to the main beam was 36 times greater than that from a single electron . This is because the waves from the six electrons in the carbon atom would all arrive ...
... single atom of say carbon , we would find that the scattered intensity close to the main beam was 36 times greater than that from a single electron . This is because the waves from the six electrons in the carbon atom would all arrive ...
Page 396
... single boundary at a single pH and ionic strength , it may still be a mixture of several components which happen to have similar mobilities under the chosen experimental conditions . It is theo- retically possible though perhaps ...
... single boundary at a single pH and ionic strength , it may still be a mixture of several components which happen to have similar mobilities under the chosen experimental conditions . It is theo- retically possible though perhaps ...
Page 437
... single zone [ 5 % bovine serum albumin in phosphate buffer ( pH 7.1 , 0.011 M ) gave a single zone ] . Accordingly , fractionation experiments to decide between interaction and heterogeneity were carried out using 10 % protein solutions ...
... single zone [ 5 % bovine serum albumin in phosphate buffer ( pH 7.1 , 0.011 M ) gave a single zone ] . Accordingly , fractionation experiments to decide between interaction and heterogeneity were carried out using 10 % protein solutions ...
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