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 418
... complex and , in fact , its area proved to be an empirical index of the extent of binding of serum albumin by pepsin . Several independent lines of evidence were presented suggesting that this complex is the spe- cific Michaelis ...
... complex and , in fact , its area proved to be an empirical index of the extent of binding of serum albumin by pepsin . Several independent lines of evidence were presented suggesting that this complex is the spe- cific Michaelis ...
Page 419
... complex between a proteolytic enzyme and its macromolecular substrate . Previously , the existence of the Michaelis- Menten complex had been shown only for low molecular weight sub- strates ( Chance , 1943 , 1951 ; Doherty and Vaslow ...
... complex between a proteolytic enzyme and its macromolecular substrate . Previously , the existence of the Michaelis- Menten complex had been shown only for low molecular weight sub- strates ( Chance , 1943 , 1951 ; Doherty and Vaslow ...
Page 433
... complex with n moles of a small uncharged constituent HA of the solvent , e.g. , undissociated buffer acid . It is assumed that the = electrophoretic mobility of the complex differs from that of the un- complexed protein and that ...
... complex with n moles of a small uncharged constituent HA of the solvent , e.g. , undissociated buffer acid . It is assumed that the = electrophoretic mobility of the complex differs from that of the un- complexed protein and that ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorbance absorption change absorption spectrum amino acids angle axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Chem chromophores coefficient concentration conformational changes contrast curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effect electric birefringence electric field electron microscope electrophoresis elution emission energy equation equilibrium excitation experimental factor film fluorescence frequency function gel filtration glycol instrument intensity interactions ionic strength ionization ions light macromolecules measured method mobility molar molecular weight molecules moving-boundary observed obtained optical parameter particles patterns peaks permanent dipole phase phenolic phenolic groups phenylalanine photomultiplier Phys polarization produced protein proton quantum yield ratio reaction relaxation residues ribonuclease rotational diffusion sample scattering shift shown in Fig solution solvent specimen spectra spectrofluorometer structure technique temperature theory tion tryptophan tyrosine ultraviolet unit cell values wavelength Weber zone