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 122
... conformation of native and denatured proteins in solution . Perturbations can be roughly divided into two classes : ( 1 ) Those produced by other groups in the protein . ( 2 ) Those produced by molecules or ions added to the protein ...
... conformation of native and denatured proteins in solution . Perturbations can be roughly divided into two classes : ( 1 ) Those produced by other groups in the protein . ( 2 ) Those produced by molecules or ions added to the protein ...
Page 129
... conformation of the protein , then in addition to the perturbation of exposed chromophores , changes in the environment of other chromophores may result . Such a conformation change , if undetected , could lead to serious errors in the ...
... conformation of the protein , then in addition to the perturbation of exposed chromophores , changes in the environment of other chromophores may result . Such a conformation change , if undetected , could lead to serious errors in the ...
Page 226
... conformational transitions do not involve all the noncovalent bonds confining a protein to the unique conformation of the native state . It is quite possible that the number of such bonds involved in a conformational change can approach ...
... conformational transitions do not involve all the noncovalent bonds confining a protein to the unique conformation of the native state . It is quite possible that the number of such bonds involved in a conformational change can approach ...
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