Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 103
... protein . In the absence of such a structural model of the protein , changes in absorp- tion can still be remarkably informative about the general type , extent , and strength of interactions of protein side chains . Although it might ...
... protein . In the absence of such a structural model of the protein , changes in absorp- tion can still be remarkably informative about the general type , extent , and strength of interactions of protein side chains . Although it might ...
Page 146
... protein . If there is no chromophore near an active site , or near a region which undergoes a conformational change , or on a surface at which ... PROTEIN ASSOCIATION When protein subunits associate , 146 JOHN W. DONOVAN F Reporter Groups.
... protein . If there is no chromophore near an active site , or near a region which undergoes a conformational change , or on a surface at which ... PROTEIN ASSOCIATION When protein subunits associate , 146 JOHN W. DONOVAN F Reporter Groups.
Page 231
... protein which has a lifetime within ~ 0.1-1 of the relaxation time of the protein . Generally the dye is bound to the protein by a covalent bond ; in some proteins it is possible to work with an adsorbed dye ( Laurence , 1952 ) . The ...
... protein which has a lifetime within ~ 0.1-1 of the relaxation time of the protein . Generally the dye is bound to the protein by a covalent bond ; in some proteins it is possible to work with an adsorbed dye ( Laurence , 1952 ) . 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