Physical Principles and Techniques of Protein Chemistry, Part 1Sydney J. Leach Physical Principles and Techniques of Protein Chemistry, Part A deals with the principles and application of selected physical methods in protein chemistry evaluation. This book is organized into nine chapters that cover microscopic, crystallographic, and electrophoretic techniques for protein conformational perturbations evaluation. This text first presents a general account of electron microscopy, its specimen preparation, optimum conditions for high resolution, measurement of electron micrographs, and illustrative examples of protein study. This book then examines the different types of map ... |
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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 - PROTEIN ASSOCIATION When protein subunits associate , 146 JOHN W. DONOVAN.
... 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 - PROTEIN ASSOCIATION When protein subunits associate , 146 JOHN W. DONOVAN.
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 ...
Page 410
... proteins and small molecules for situations in which the protein is acid to its iso- electric point ( with positive mobilities and the mobility of the complexed protein molecule being assumed greater than that of the uncomplexed protein ) ...
... proteins and small molecules for situations in which the protein is acid to its iso- electric point ( with positive mobilities and the mobility of the complexed protein molecule being assumed greater than that of the uncomplexed protein ) ...
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ions lens light linear macromolecules 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 unit cell values wavelength Weber Winzor zone