## 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
Circular dichroism of the “random” polypeptide chain
✍ Scribed by M. Lois Tiffany; S. Krimm
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1969
- Tongue
- English
- Weight
- 674 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
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 now obtained CD spectra of the unordered forms of the above synthetic polypeptides, as well as of two fibrous proteins (collagen and feather keratin) and a globular protein (myoglobin). These spectra are all similar to that of unordered polyproline, having a negative band in the vicinity of 200 ma and no additional bands at longer wavelengths. The lack of structural uniqueness of the unordered polypeptide chain is emphasized by these studies.
📜 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 28‐mer 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
The hydrogen-tritium exchange character of poly-D,L-alanine was studied in detail aa a model for the hydrogen exchange behavior of the unhindered, polymeric peptide group. The random chain nature of poly-D,L-alanine was evident in the uniformity of exchange rate of all its hydrogens and in the simil
## Abstract The 218‐nm peak, characteristic of the circular dichroism of randomly coiled poly‐α‐amino acids can be demonstrated in solutions of penta‐L‐lysine, α‐glycyl‐L‐lysine, as well as poly‐L‐lysine. The thermal stability of the particular state that gives rise to this 218‐nm band in the CD is