Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 109
... solvent " may be hydrocarbon - like . Or the " solvent " may be highly polarizable , such as the immediate environment of tyrosine residue 97 in ribonuclease which contains two disulfide bonds . In pro- teins , " mixed " solvent ...
... solvent " may be hydrocarbon - like . Or the " solvent " may be highly polarizable , such as the immediate environment of tyrosine residue 97 in ribonuclease which contains two disulfide bonds . In pro- teins , " mixed " solvent ...
Page 110
... solvent molecules is called the orientation shift . Two other interactions between chromophores and solvent occur . The first and most ubiquitous is the London dispersion interaction , the polari- zation of the electron distribution of ...
... solvent molecules is called the orientation shift . Two other interactions between chromophores and solvent occur . The first and most ubiquitous is the London dispersion interaction , the polari- zation of the electron distribution of ...
Page 129
... solvent perturbation technique was introduced by Herskovits and Laskowski ( 1960 ) . In this procedure , chromophores which are in contact with the solvent are de- liberately perturbed by addition of another solvent component . In the ...
... solvent perturbation technique was introduced by Herskovits and Laskowski ( 1960 ) . In this procedure , chromophores which are in contact with the solvent are de- liberately perturbed by addition of another solvent component . In 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