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 38
... observation of individual freeze- dried macromolecules . These small particles simply disappear during sublimation . Westerberg ( 1961 ) has , however , observed freeze - dried strands of DNA , and it is possible that in the future ...
... observation of individual freeze- dried macromolecules . These small particles simply disappear during sublimation . Westerberg ( 1961 ) has , however , observed freeze - dried strands of DNA , and it is possible that in the future ...
Page 50
... observed after its activation by thrombin and subsequent polymerization to form fibrin . An apparent difficulty is raised by the observation of fibrinogen molecules as long as 475 Å be- cause the periodicity of fibrin is only 230 Å . As ...
... observed after its activation by thrombin and subsequent polymerization to form fibrin . An apparent difficulty is raised by the observation of fibrinogen molecules as long as 475 Å be- cause the periodicity of fibrin is only 230 Å . As ...
Page 51
... observed in the pH range from 4.0 to 3.6 . Over the same pH range , a decrease of sedimentation constant and diffusion co- efficient , and an increase in intrinsic viscosity are observed . At neutral pH , however , the bovine serum ...
... observed in the pH range from 4.0 to 3.6 . Over the same pH range , a decrease of sedimentation constant and diffusion co- efficient , and an increase in intrinsic viscosity are observed . At neutral pH , however , the bovine serum ...
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