Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 52
However, the appearance of bovine serum albumin preparations in electron
micrographs is not a true representation of the conformation of molecules in
solution. At best, about half of the molecules are seen to have undergone some
degree of ...
However, the appearance of bovine serum albumin preparations in electron
micrographs is not a true representation of the conformation of molecules in
solution. At best, about half of the molecules are seen to have undergone some
degree of ...
Page 238
the interaction of ANS with bovine serum albumin has been accomplished
recently by Weber and co-workers. Five molecules of ANS are bound with
constant quantum yield though they are not uniformly distributed on the surface (
Daniel and ...
the interaction of ANS with bovine serum albumin has been accomplished
recently by Weber and co-workers. Five molecules of ANS are bound with
constant quantum yield though they are not uniformly distributed on the surface (
Daniel and ...
Page 323
In Jacobsen's treatment, protein molecules are represented by a hole surrounded
by a thick layer of quasicrystalline water. However, simple analyses show that
this may not be an appropriate model for protein molecules in solution. Thus, the
...
In Jacobsen's treatment, protein molecules are represented by a hole surrounded
by a thick layer of quasicrystalline water. However, simple analyses show that
this may not be an appropriate model for protein molecules in solution. Thus, the
...
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Contents
Electron Microscopy | 2 |
Dielectric Properties of Proteins | 7 |
Operational Requirements for HighResolution Electron | 15 |
Copyright | |
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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