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 262
... interactions 108-109 ~ 102-104 T , P , D , S Hydrophobic interactions Binding of charged dyese to proteins 106-5 X 108 to nucleic acids ~ 106-108 Enzyme - substrate ~ 107-108 102-104 ~ 102-104 102-104 T T , C T , C and antibody- hapten ...
... interactions 108-109 ~ 102-104 T , P , D , S Hydrophobic interactions Binding of charged dyese to proteins 106-5 X 108 to nucleic acids ~ 106-108 Enzyme - substrate ~ 107-108 102-104 ~ 102-104 102-104 T T , C T , C and antibody- hapten ...
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 ...
Contents
Electron Microscopy of Globular Proteins | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Copyright | |
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absorption absorption spectrum amino acids applied axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration conformational changes contrast curve Debye 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 energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ionization ions light macromolecules measured method migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic Phys plot polarization polymer produced protein proton quantum yield ratio reaction relaxation residues resolution ribonuclease shown in Fig solution solvent specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone