Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 7
Absorption contrast is enhanced in stained specimens . ... the light microscope ,
differences in refractive index and / or thickness between regions of the specimen
are systematically exploited in the production of differences in image intensity .
Absorption contrast is enhanced in stained specimens . ... the light microscope ,
differences in refractive index and / or thickness between regions of the specimen
are systematically exploited in the production of differences in image intensity .
Page 25
6a , is the quantity ( 3 ) horizontal distance of evaporation source from specimen
vertical distance of evaporation source above specimen In principle , this quantity
should be equal to the effective shadow ratio , which is length of shadow cast ...
6a , is the quantity ( 3 ) horizontal distance of evaporation source from specimen
vertical distance of evaporation source above specimen In principle , this quantity
should be equal to the effective shadow ratio , which is length of shadow cast ...
Page 46
Calibration Specimens An ideal calibration specimen contains regular spacings
which are known precisely by means which are independent of electron
microscopy , and which , ideally , should be comparable in size to the objects to
be ...
Calibration Specimens An ideal calibration specimen contains regular spacings
which are known precisely by means which are independent of electron
microscopy , and which , ideally , should be comparable in size to the objects to
be ...
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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 concentration constant containing contrast corrected corresponding curve decrease dependence determined dielectric difference diffusion dipole direction discussed distribution effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor fluorescence fraction frequency function given groups Herskovits important increase indicates intensity interactions ionic ions length light limited macromolecules measured method mobility molecular molecules observed obtained occurs optical orientation particles patterns peaks perturbation phase phenolic polarization position possible preparation present produced protein quantum range ratio reaction reference relative relaxation respectively rotation sample separation serum albumin shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion transfer transition tryptophan unit usually volume wavelength yield zone