Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 110
... interactions between oriented chromophore and 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 ...
... interactions between oriented chromophore and 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 ...
Page 411
... Interaction of Macromolecules with Small Ions Another important type of interaction shown by proteins in solution is the binding of ions other than H + . Since the binding of salt ions by a protein should change its net charge , its ...
... Interaction of Macromolecules with Small Ions Another important type of interaction shown by proteins in solution is the binding of ions other than H + . Since the binding of salt ions by a protein should change its net charge , its ...
Page 438
... interaction of bovine serum albumin with borate buffer and are not due to inherent heterogeneity . The phenomenon of multiple zones due to reversible protein - buffer interaction is not unique for bovine serum albumin . Thus ...
... interaction of bovine serum albumin with borate buffer and are not due to inherent heterogeneity . The phenomenon of multiple zones due to reversible protein - buffer interaction is not unique for bovine serum albumin . Thus ...
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