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 83
... peaks appear close to the true positions of the lighter atoms . The peaks associated with the hydrogen atoms are very weak and are lost in the spurious background . The accuracy of the map can be improved by Fourier refinement . In ...
... peaks appear close to the true positions of the lighter atoms . The peaks associated with the hydrogen atoms are very weak and are lost in the spurious background . The accuracy of the map can be improved by Fourier refinement . In ...
Page 405
... peaks even for very rapid reequili- bration . The implications for conventional electrophoretic analysis have already been touched upon and will be developed more fully below . Finally , the new understanding provided by these ...
... peaks even for very rapid reequili- bration . The implications for conventional electrophoretic analysis have already been touched upon and will be developed more fully below . Finally , the new understanding provided by these ...
Page 418
... peaks , a fast - moving bound- ary corresponding to pure A and a bimodal reaction boundary across which C and B disappear and the concentration of A changes markedly . An example ( Cann and Klapper , 1961 ) of the predicted behavior is ...
... peaks , a fast - moving bound- ary corresponding to pure A and a bimodal reaction boundary across which C and B disappear and the concentration of A changes markedly . An example ( Cann and Klapper , 1961 ) of the predicted behavior is ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
Operational Requirements for HighResolution Electron | 15 |
Copyright | |
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absorbance absorption change absorption spectrum amino acids angle axis binding 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