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Effects of Local Environment on the Circular Dichroism Spectra of Polypeptides

✍ Scribed by M. Cascio; B.A. Wallace


Publisher
Elsevier Science
Year
1995
Tongue
English
Weight
800 KB
Volume
227
Category
Article
ISSN
0003-2697

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πŸ“œ SIMILAR VOLUMES


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## Abstract The circular dichroism (CD) spectra of poly‐L‐proline and of poly‐L‐glutamic acid and poly‐L‐lysine in their charged states have been studied as a function of temperature. The variation of CD spectra with temperature is inconsistent with the assignment of the spectrum of such charged po

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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

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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

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## 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