Physical Principles and Techniques of Protein Chemistry, Part 1 |
From inside the book
Results 1-3 of 99
Page 115
Although it appears that accurate calculation of the a - helical content of a protein
from its absorption in the 190 mu region cannot now be carried out , a change in
absorption at 190 mu can still be used as a measure of conformational change .
Although it appears that accurate calculation of the a - helical content of a protein
from its absorption in the 190 mu region cannot now be carried out , a change in
absorption at 190 mu can still be used as a measure of conformational change .
Page 123
the sedimentation coefficient of ovomucoid is essentially unchanged between pH
1 and pH 12 ; ( 2 ) the difference spectrum obeyed Beer ' s law , so that the molar
difference absorption coefficient was concentration - independent ; ( 3 ) solvent ...
the sedimentation coefficient of ovomucoid is essentially unchanged between pH
1 and pH 12 ; ( 2 ) the difference spectrum obeyed Beer ' s law , so that the molar
difference absorption coefficient was concentration - independent ; ( 3 ) solvent ...
Page 139
an average absorption change of A€292 = – 1600 per indole group ( Donovan ,
1964 ) . Comparison of the perturbation produced by the protein interior with the
perturbation produced by 20 % ethylene glycol indicates that the interior of a ...
an average absorption change of A€292 = – 1600 per indole group ( Donovan ,
1964 ) . Comparison of the perturbation produced by the protein interior with the
perturbation produced by 20 % ethylene glycol indicates that the interior of a ...
What people are saying - Write a review
We haven't found any reviews in the usual places.
Contents
SLAYTER | 2 |
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Copyright | |
48 other sections not shown
Other editions - View all
Common terms and phrases
absorption acid albumin appears applied atoms axis birefringence boundary buffer calculated cell charge Chem chromophores complex concentration constant containing contrast corrected corresponding curve dependence determined dielectric difference diffusion dipole direction discussed distribution effects electric electric field electron electrophoresis elution emission energy equation equilibrium example excitation experimental experiments factor field flow fluorescence fraction frequency function gel filtration given groups important increase indicates intensity interactions ionic ions length light limited macromolecules measured method microscope migration mobility molecular molecules observed obtained occurs optical particles patterns peaks perturbation phase plot polarization position possible preparation present produced protein range ratio reaction reference relative relaxation resolution respectively rotation separation serum shift shown single solution solvent specimen spectra spectrum strength structure studies technique theory tion unit usually values volume wavelength weight yield zone