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

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Page 104

Here, A is the

lowest vibrational level of the ground state and ... B and C are the

the respective vibrations, and n and m are the number of quanta of these

vibrations ...

Here, A is the

**frequency**corresponding to the energy difference between thelowest vibrational level of the ground state and ... B and C are the

**frequencies**ofthe respective vibrations, and n and m are the number of quanta of these

vibrations ...

Page 303

I | a *T* ( ) where e, and e. are the dielectric constants at very low and very high

the ordinate in (a) is the real part of the complex dielectric constant and in (b) is

the ...

I | a *T* ( ) where e, and e. are the dielectric constants at very low and very high

**frequencies**, respectively. ... The abscissa is the logarithm of the**frequency**andthe ordinate in (a) is the real part of the complex dielectric constant and in (b) is

the ...

Page 309

Another cause of error is due to an inductance (Schwan, 1963) and this becomes

serious at higher

the specific conductivity k of the solution at each

Another cause of error is due to an inductance (Schwan, 1963) and this becomes

serious at higher

**frequencies**. ... we may calculate the dielectric constant e andthe specific conductivity k of the solution at each

**frequency**(60) C = ee,(A/l) (62) ...### What people are saying - Write a review

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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