Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 127
... group . At 234 mu , Ae for the carboxyl dissociation is negative , and that for the amino group positive , while at 228 mu , both groups produce a positive Ae . No absorption changes at all are observed at 287 mu , an isosbestic point ...
... group . At 234 mu , Ae for the carboxyl dissociation is negative , and that for the amino group positive , while at 228 mu , both groups produce a positive Ae . No absorption changes at all are observed at 287 mu , an isosbestic point ...
Page 145
... groups is 286.0 — 0.3 = 285.7 mp , which is 0.7 mu to the red of the model compound acetyl- tyrosine ethyl ester ... groups are titrated , it is possible that this is an example of a direct charge effect of an imidazole group upon a ...
... groups is 286.0 — 0.3 = 285.7 mp , which is 0.7 mu to the red of the model compound acetyl- tyrosine ethyl ester ... groups are titrated , it is possible that this is an example of a direct charge effect of an imidazole group upon a ...
Page 146
... group may be reflected in changes in its absorption ( or fluores- cence , or EPR , NMR , or other characteristic signal which can be ob- tained from it ) . There are three important considerations in the use of chromophores as reporter ...
... group may be reflected in changes in its absorption ( or fluores- cence , or EPR , NMR , or other characteristic signal which can be ob- tained from it ) . There are three important considerations in the use of chromophores as reporter ...
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