Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 42
Instrumental magnification is obtained by calibration , as discussed in Section V ,
C . The print magnification is set approximately in making the enlargement , but
when precise measurements are required it should be determined exactly by a ...
Instrumental magnification is obtained by calibration , as discussed in Section V ,
C . The print magnification is set approximately in making the enlargement , but
when precise measurements are required it should be determined exactly by a ...
Page 47
Diameters obtained from measurements of shadow - cast particles must be
corrected by an empirical factor of the order of 50 Å , which compensates for the
accumulation of shadowing metal . Particle height measurements from shadow -
cast ...
Diameters obtained from measurements of shadow - cast particles must be
corrected by an empirical factor of the order of 50 Å , which compensates for the
accumulation of shadowing metal . Particle height measurements from shadow -
cast ...
Page 486
the second solute may be obtained using Eq . ( 22 ) and the known values of VA ,
Vp and K ' n for the first solute . For unequivocal interpretation of CAVw in terms
of differences between the values of K ' n for the two proteins , a combination of ...
the second solute may be obtained using Eq . ( 22 ) and the known values of VA ,
Vp and K ' n for the first solute . For unequivocal interpretation of CAVw in terms
of differences between the values of K ' n for the two proteins , a combination of ...
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Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to the Study | 48 |
Copyright | |
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absorbance absorption acid appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores complex components concentration constant containing corrected corresponding curve dependence determined dielectric difference diffusion dipole direction distribution effect electric field electron electrophoresis elution emission energy equation equilibrium et al example excitation experimental experiments factor flow fluorescence fraction frequency function gel filtration given groups important increase indicate intensity interactions interpretation ionic strength ions light limited macromolecules measured method migration mixture mobility molecular molecules moving-boundary observed obtained occurs optical orientation particles patterns peaks perturbation phase plot polarization position possible present procedure produced protein ratio reaction reference relative relaxation respectively rotational separation serum albumin shown single solution solvent specific spectra spectrum structure studies technique theoretical theory tion unit usually values volume wavelength weight yield zone