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

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Page 60

... value of the Patterson

cylindrical polar coordinates in real space P pitch of a helix u/t description of a

helix with u units in t turns R, W, Z cylindrical polar coordinates in reciprocal

space I(R, ...

... value of the Patterson

**function**at the point r, y, z V volume of unit cell r, b, 2cylindrical polar coordinates in real space P pitch of a helix u/t description of a

helix with u units in t turns R, W, Z cylindrical polar coordinates in reciprocal

space I(R, ...

Page 328

#!/s. m°G(n) dry (86) where Brio represents the relaxation time, G (m) is a

distribution

parameter a such that a = m/mo (mo is an arbitrary number) and introducing a

new

#!/s. m°G(n) dry (86) where Brio represents the relaxation time, G (m) is a

distribution

**function**, and Aet is the total dielectric increment. Defining a newparameter a such that a = m/mo (mo is an arbitrary number) and introducing a

new

**function**...Page 329

_ _ exp [(s – t)/3] 16-0 – Horto, (90) We can rewrite the

oxp(s) = (F) s. g(t)h(s – t) dt (91) Eq. (91) can be rewritten in terms of the Fourier

transformation of g(t), h(s), and p(s), namely G(r), H(r), and p(r) + (r”) Using the ...

_ _ exp [(s – t)/3] 16-0 – Horto, (90) We can rewrite the

**function**p(s) as follows 1oxp(s) = (F) s. g(t)h(s – t) dt (91) Eq. (91) can be rewritten in terms of the Fourier

transformation of g(t), h(s), and p(s), namely G(r), H(r), and p(r) + (r”) Using the ...

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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