Physical principles and techniques of protein chemistry, Part 1 |
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Page 37
The protective effect of the negative contrast method of course depends upon a
choice of pH and composition of the contrasting medium which is compatible with
the stability of the specimen. C. Embedding The methods of fixation, embedding,
...
The protective effect of the negative contrast method of course depends upon a
choice of pH and composition of the contrasting medium which is compatible with
the stability of the specimen. C. Embedding The methods of fixation, embedding,
...
Page 85
D. The Method of Isomorphous Replacement The heavy atom method described
in the previous section cannot be used to determine the structure of globular
protein crystals because even the heaviest atom would not have sufficient weight
to ...
D. The Method of Isomorphous Replacement The heavy atom method described
in the previous section cannot be used to determine the structure of globular
protein crystals because even the heaviest atom would not have sufficient weight
to ...
Page 279
B. Flow Devices Flow methods may he used in the time range from about 1 msec
to about 1 minute. They differ in their economy of reactant solution, time
resolution, and simplicity, i.e., in cost and convenience, but they are
characterized by a ...
B. Flow Devices Flow methods may he used in the time range from about 1 msec
to about 1 minute. They differ in their economy of reactant solution, time
resolution, and simplicity, i.e., in cost and convenience, but they are
characterized by a ...
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Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to | 48 |
Copyright | |
47 other sections not shown
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Common terms and phrases
absorbance absorption change absorption spectrum amino acids applied axis binding Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann carboxyl Chem chromophores coefficient components concentration conformational changes contrast curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole Edelhoch effect electric birefringence electric field electron microscope electrophoresis elution volume emission energy enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration glycol gradient heavy atom 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 phase phenolic phenolic groups photomultiplier Phys plot polarization polymer produced proton quantum yield ratio reaction relaxation residues resolution ribonuclease sample shadow shift shown in Fig solvent solvent perturbation specimen spectra structure technique temperature theoretical theory tion tryptophan tyrosine ultraviolet unit cell values wavelength Weber