## Physical Principles and Techniques of Protein Chemistry, Part 1 |

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Page 405

Theoretical moving-boundary electrophoretic

for K” = 10°, n = 3 and values of C2.0/C, o given below. —, gradient curves; ---,

pHA. Virtually the same results were obtained for n = 1, the only differences being

...

Theoretical moving-boundary electrophoretic

**patterns**(Cann and Goad, 1965a)for K” = 10°, n = 3 and values of C2.0/C, o given below. —, gradient curves; ---,

pHA. Virtually the same results were obtained for n = 1, the only differences being

...

Page 406

Theoretical moving-boundary electrophoretic

for K” = 10°, Cao/C1.0 - 1 and values of n shown opposite the

gradient curves; ---, pHA. For n = 3, time of electrophoresis = 1.72 X 10." sec. For

n = 10 ...

Theoretical moving-boundary electrophoretic

**patterns**(Cann and Goad, 1965a)for K” = 10°, Cao/C1.0 - 1 and values of n shown opposite the

**patterns**. —,gradient curves; ---, pHA. For n = 3, time of electrophoresis = 1.72 X 10." sec. For

n = 10 ...

Page 408

Compare, for example, the theoretical

with the experimental ones shown in Fig. 11 for 0.04 M sodium formate buffer.

Indeed, the particular type of nonenantiography displayed by these

...

Compare, for example, the theoretical

**patterns**presented in Fig. 15 for n = 30with the experimental ones shown in Fig. 11 for 0.04 M sodium formate buffer.

Indeed, the particular type of nonenantiography displayed by these

**patterns**(two...

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### Contents

Electron Microscopy | 2 |

Dielectric Properties of Proteins | 7 |

Operational Requirements for HighResolution Electron | 15 |

Copyright | |

32 other sections not shown

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### Common terms and phrases

absorbance absorption acid albumin appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores concentration constant containing contrast corrected corresponding curve dependence determined dielectric difference diffusion dipole direction effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor field flow fluorescence fraction frequency function given groups important increase indicates intensity interactions ionic ions length light limited macromolecules measured method microscope mobility molecular molecules observed obtained occurs optical particles patterns peaks perturbation phase polarization position possible preparation present produced protein range ratio reaction reference relative relaxation resolution respectively rotation sample separation serum shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion tryptophan unit usually values volume wavelength weight yield zone