Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 109
... chromophores , it is necessary to consider in detail the effect of solvents on chromophores . Solvents alter the intensity of absorption of a chromophore and shift its absorption spectrum along the wavelength scale . The change is de ...
... chromophores , it is necessary to consider in detail the effect of solvents on chromophores . Solvents alter the intensity of absorption of a chromophore and shift its absorption spectrum along the wavelength scale . The change is de ...
Page 130
... chromophores exposed to water at the surface of a protein molecule are " red - shifted " relative to the vapor spectrum , be- cause of the polarization red shift described above ( Section II , B ) . By changing the composition of the ...
... chromophores exposed to water at the surface of a protein molecule are " red - shifted " relative to the vapor spectrum , be- cause of the polarization red shift described above ( Section II , B ) . By changing the composition of the ...
Page 138
... chromophores exposed to the solvent in the native protein ( from the initial rate of change of absorption with perturbant concentration ) and the number of chromophores released to the solvent in the denaturation process ( from the ...
... chromophores exposed to the solvent in the native protein ( from the initial rate of change of absorption with perturbant concentration ) and the number of chromophores released to the solvent in the denaturation process ( from the ...
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