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 of polypeptide monolayers
β Scribed by Donald G Cornell
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 995 KB
- Volume
- 70
- Category
- Article
- ISSN
- 0021-9797
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The secondary structure of abductin was investigated by CD and NMR studies of several synthetic peptides. Results obtained with these peptides showed the dominant conformations to be the polyproline II (PPII) structure in aqueous solution and different types of b-turns in the less polar solvent trif
## 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
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