Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 40
Consequently, electron microscope preparations of macromolecules tend to
appear misleadingly homogeneous in terms of molecular weight. Even the linear
dimensions of a group of small spheres of different sizes tend to seem uniform to
the ...
Consequently, electron microscope preparations of macromolecules tend to
appear misleadingly homogeneous in terms of molecular weight. Even the linear
dimensions of a group of small spheres of different sizes tend to seem uniform to
the ...
Page 170
SUPPLEMENTARY READINGs I. MOLECULAR SPECTROSCOPY Barrow, G. M.
(1962). “Introduction to Molecular Spectroscopy” McGraw-Hill New York. Barrow,
G. M. (1963). “The Structure of Molecules” Benjamin, New York. Beaven, G. H. ...
SUPPLEMENTARY READINGs I. MOLECULAR SPECTROSCOPY Barrow, G. M.
(1962). “Introduction to Molecular Spectroscopy” McGraw-Hill New York. Barrow,
G. M. (1963). “The Structure of Molecules” Benjamin, New York. Beaven, G. H. ...
Page 472
Furthermore, it should be realized that molecular weights obtained from s” and
D9 are subject to considerably greater experimental error than those derived
from techniques such as light scattering and equilibrium sedimentation. A method
of ...
Furthermore, it should be realized that molecular weights obtained from s” and
D9 are subject to considerably greater experimental error than those derived
from techniques such as light scattering and equilibrium sedimentation. A method
of ...
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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