Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 138
... denaturation process ( from the final slope of the change in absorption with perturbant concentration , and from the mag- nitude of the absorption decrease on denaturation ) . However , since many proteins appear to have partially ...
... denaturation process ( from the final slope of the change in absorption with perturbant concentration , and from the mag- nitude of the absorption decrease on denaturation ) . However , since many proteins appear to have partially ...
Page 139
... denaturation of pro- teins usually produces a much larger change in absorption near 230 mμ than near 280 mp . Some of this change in absorption may be produced by changes in the n → absorption of the amide bonds in the protein , either ...
... denaturation of pro- teins usually produces a much larger change in absorption near 230 mμ than near 280 mp . Some of this change in absorption may be produced by changes in the n → absorption of the amide bonds in the protein , either ...
Page 140
... denaturation curves for ribonuclease shown in Fig . 15. When K has been determined as a function of temperature , other thermodynamic quantities may be obtained by use of Eqs . ( 8 ) – ( 10 ) . " The validity of the " two - state ...
... denaturation curves for ribonuclease shown in Fig . 15. When K has been determined as a function of temperature , other thermodynamic quantities may be obtained by use of Eqs . ( 8 ) – ( 10 ) . " The validity of the " two - state ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
Dielectric Properties of Proteins | 7 |
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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