Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 148
Determination of Tyrosine and Tryptophan Since tryptophan is destroyed during
the acid hydrolysis used in preparing samples for amino acid analysis , it is more
convenient to determine the tryptophan content from the ultraviolet absorption of
...
Determination of Tyrosine and Tryptophan Since tryptophan is destroyed during
the acid hydrolysis used in preparing samples for amino acid analysis , it is more
convenient to determine the tryptophan content from the ultraviolet absorption of
...
Page 151
determined from the absorption of the protein measured at 288 and 280 mu 6288
= 4815M Trp + 385M Tyr ( 17 ) €280 = 5690M Trp + 1280M Tyr The absorption
coefficients for tyrosine and tryptophan used in these equations were determined
...
determined from the absorption of the protein measured at 288 and 280 mu 6288
= 4815M Trp + 385M Tyr ( 17 ) €280 = 5690M Trp + 1280M Tyr The absorption
coefficients for tyrosine and tryptophan used in these equations were determined
...
Page 354
The pulse duration is determined by the length of the cable . With a 500 - foot
cable and a high voltage power supply , the apparatus generated pulses of 1 . 7
usec duration and variable amplitude to 8 kV . It was used for studying the Kerr ...
The pulse duration is determined by the length of the cable . With a 500 - foot
cable and a high voltage power supply , the apparatus generated pulses of 1 . 7
usec duration and variable amplitude to 8 kV . It was used for studying the Kerr ...
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Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to the Study | 48 |
Copyright | |
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Common terms and phrases
absorbance absorption acid appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores complex concentration constant containing contrast corrected corresponding curve decrease dependence determined dielectric difference diffusion dipole direction discussed distribution effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor fluorescence fraction frequency function given groups Herskovits important increase indicates intensity interactions ionic ions length light limited macromolecules measured method mobility molecular molecules observed obtained occurs optical orientation particles patterns peaks perturbation phase phenolic polarization position possible preparation present produced protein quantum range ratio reaction reference relative relaxation respectively rotation sample separation serum albumin shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion transfer transition tryptophan unit usually volume wavelength yield zone