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 235
... interactions in the excited state of the dye . 4. Unfolded States The native state of globular proteins appears to be one which is char- acterized by a maximum number of intramolecular interactions . The X - ray analysis of the ...
... interactions in the excited state of the dye . 4. Unfolded States The native state of globular proteins appears to be one which is char- acterized by a maximum number of intramolecular interactions . The X - ray analysis of the ...
Page 440
... interactions . A relatively easy method for detecting reversible interactions has been devised by Naka- mura et al . ( 1959 ) . Their method , which is an adaptation of conventional paper electrophoresis , is referred to as crossing ...
... interactions . A relatively easy method for detecting reversible interactions has been devised by Naka- mura et al . ( 1959 ) . Their method , which is an adaptation of conventional paper electrophoresis , is referred to as crossing ...
Page 493
... interactions involving unstable proteins such as the proteolytic enzymes , while the latter would prove useful in the study of rapid equilibria involving proteins and large macromole- cules , e.g. , viruses or nucleic acids . At this ...
... interactions involving unstable proteins such as the proteolytic enzymes , while the latter would prove useful in the study of rapid equilibria involving proteins and large macromole- cules , e.g. , viruses or nucleic acids . At this ...
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