The circular dichroism (CD) spectrum of an unordered polypeptide chain does not correspond, as has been assumed heretofore, to that of a charged chain such as poly-~glutamic acid or poly-clysine. The latter have been shown to have locally ordered structures with characteristic CD spectra. We have no
Circular dichroism calculation for random-coil polypeptide chains
β Scribed by V. A. Zubkov; T. M. Birshtein; I. S. Milevskaya; M. V. Volkenstein
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1971
- Tongue
- English
- Weight
- 550 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Synopsis
A ~netliod of calculation of the circular dichroism (CD) of random-coil polypeptides hw been developed by means of a illonte-Carlo approarh to the treatment of statistical systems and exciton theory of optical activity of polymers. The contribution of r-r* and n-r* amide transitions to the CII has been taken into account. The r-r* transition gives rise to two CD bands: a negative short-wavelength band and a weak positive long-wavelength one. The n-r* transition gives rise to one negative CD band.
π SIMILAR VOLUMES
## Abstract A calculation has been done of the circular dichroism (CD) spectrum of an unordered polypeptide chain. This has been based on a Boltzmann averaging over a dipeptide conformational CD map. This is shown to be valid by comparing the CD spectra of 28βmer oligopeptides with those generated
We have measured the VCD of polytyrosine in the amide I and I1 regions in dimethyl sulfoxide (DMSO) and in 8020 mixtures of DMSO with trifluoroethanol, trifluoroacetic acid (TFA), and dichloroacetic acid and in 50:50 mixtures of DMSO and trimethyl phosphate (TMP). Additionally, VCD was obtained for
## Abstract Recent experiments have shown that the circular dichroism of polyβLβproline II is negative from 130 to 220 nm. Therefore, calculations based on exciton interactions alone cannot give the observed spectrum. The present calculations were carried out in the framework of the randomβphase a
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