Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 154
... absorbance ( that absorbance giving the smallest relative error of measurement ) with a shot - noise limited system is about 1.0 ( Fig . 21 ) . However , samples with absorb- ances of 2 or 3 are measured nearly as accurately . 0.12 ...
... absorbance ( that absorbance giving the smallest relative error of measurement ) with a shot - noise limited system is about 1.0 ( Fig . 21 ) . However , samples with absorb- ances of 2 or 3 are measured nearly as accurately . 0.12 ...
Page 156
... absorbance at 275 mμ of successive pairs of K2CrO , solutions ( ordinate ) , plotted against the true absorbance of the more concentrated solution ( abscissa ) . O , Measurements made with the Cary 14 spectrophotometer ; measurements ...
... absorbance at 275 mμ of successive pairs of K2CrO , solutions ( ordinate ) , plotted against the true absorbance of the more concentrated solution ( abscissa ) . O , Measurements made with the Cary 14 spectrophotometer ; measurements ...
Page 158
... absorbance units.12 Many good spectrophotometers will give an accuracy and reproducibility of 0.0002 absorbance units , so that an absorbance difference of 0.02 can be measured with 1 % accuracy . If spectra are recorded slowly , using ...
... absorbance units.12 Many good spectrophotometers will give an accuracy and reproducibility of 0.0002 absorbance units , so that an absorbance difference of 0.02 can be measured with 1 % accuracy . If spectra are recorded slowly , using ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
Dielectric Properties of Proteins | 7 |
Copyright | |
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absorption absorption spectrum amino acids applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann cell Chem chromophores coefficient components concentration curve Debye denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission enzyme equation equilibrium excitation experimental film fluorescence fraction frequency gel filtration gradient groups instrument intensity interactions ionic strength ions lens light linear macromolecules magnification 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 values wavelength Weber Winzor zone