Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 125
Sydney J. Leach. A. PERTURBATION BY CHARGED GROUPS Chromophores in a protein can be perturbed by adjacent positive or negative charges . Their spectra may thereby be altered . Experimentally , as the negative charge is increased , it is ...
Sydney J. Leach. A. PERTURBATION BY CHARGED GROUPS Chromophores in a protein can be perturbed by adjacent positive or negative charges . Their spectra may thereby be altered . Experimentally , as the negative charge is increased , it is ...
Page 128
... charge effect , since the effect of the charge is indirect . Experimentally , it is very difficult to rule out indirect effects when the perturbation of a chromophore is observed to be controlled by the ionization of another side ...
... charge effect , since the effect of the charge is indirect . Experimentally , it is very difficult to rule out indirect effects when the perturbation of a chromophore is observed to be controlled by the ionization of another side ...
Page 376
... charge inside this surface . This charge is not necessarily identical with the net charge of the particle , since some of the ions of the ionic atmos- phere may be present within the surface of shear , thereby reducing the electrophoretic ...
... charge inside this surface . This charge is not necessarily identical with the net charge of the particle , since some of the ions of the ionic atmos- phere may be present within the surface of shear , thereby reducing the electrophoretic ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
Dielectric Properties of Proteins | 7 |
Copyright | |
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absorption absorption spectrum amino acids applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann cell Chem chromophores coefficient components concentration curve Debye denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission enzyme equation equilibrium excitation experimental film fluorescence fraction frequency gel filtration gradient groups instrument intensity interactions ionic strength ions lens light linear macromolecules magnification measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine values wavelength Weber Winzor zone