Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 62
If a number of atoms were combined together to form a molecule, the scattered
intensity would no longer be cylindrically symmetrical about the main beam.
Instead its intensity would fluctuate, being large in directions in which the waves ...
If a number of atoms were combined together to form a molecule, the scattered
intensity would no longer be cylindrically symmetrical about the main beam.
Instead its intensity would fluctuate, being large in directions in which the waves ...
Page 172
... 2, 3) pi 0, 0. intensity of emitted radiation (in terms of quanta emitted in unit time
) probability of spontaneous transition number of excited molecules at equilibrium
“natural” lifetime of the excited state in the absence of perturbations transition ...
... 2, 3) pi 0, 0. intensity of emitted radiation (in terms of quanta emitted in unit time
) probability of spontaneous transition number of excited molecules at equilibrium
“natural” lifetime of the excited state in the absence of perturbations transition ...
Page 189
B. FLUoRESCENCE PARAMETERs 1. Intensity While the intensity of
fluorescence of a sample can be measured exactly, for many purposes it is
sufficient merely to obtain a quantity, the “observed fluorescence intensity,”
expressed in arbitrary ...
B. FLUoRESCENCE PARAMETERs 1. Intensity While the intensity of
fluorescence of a sample can be measured exactly, for many purposes it is
sufficient merely to obtain a quantity, the “observed fluorescence intensity,”
expressed in arbitrary ...
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Contents
Electron Microscopy | 2 |
Dielectric Properties of Proteins | 7 |
Operational Requirements for HighResolution Electron | 15 |
Copyright | |
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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