Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 140
... temperature , a measure of the amount of denatured protein present , can be used to determine the equilibrium constant for the de- naturation process at that temperature , provided that the usual thermo- dynamic criteria ( known initial ...
... temperature , a measure of the amount of denatured protein present , can be used to determine the equilibrium constant for the de- naturation process at that temperature , provided that the usual thermo- dynamic criteria ( known initial ...
Page 225
... temperature range show a continuous decrease in fluorescence with increasing temperature . The fluorescence of tryptophan and tyrosine residues which are buried is probably un- affected , or only slightly affected , by temperature ...
... temperature range show a continuous decrease in fluorescence with increasing temperature . The fluorescence of tryptophan and tyrosine residues which are buried is probably un- affected , or only slightly affected , by temperature ...
Page 288
... Temperature - Jump Techniques Some reactions involving proteins are characterized by equilibria which are displaced far over in the direction of the products . In cases where the velocities are too high for measurement by flow methods ...
... Temperature - Jump Techniques Some reactions involving proteins are characterized by equilibria which are displaced far over in the direction of the products . In cases where the velocities are too high for measurement by flow methods ...
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