Ultraviolet circular dichroism of polyproline and oriented collagen
β Scribed by Richard Mandel; George Holzwarth
- Book ID
- 102760289
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 991 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The ultraviolet absorption, linear dichroism, circular dichroism, and oriented circular dichroism of collagen are reported and the spectra are resolved into a selfβconsistent set of bands in accord with exciton theory. The parallel band at 200 nm has 40% of the Ο β Ο* intensity; the perpendicular band is placed at 189 nm yielding a splitting of 2700 cm^β1^. The circular dichroism is resolved into two Gaussians at Ξ»~β₯~ and Ξ»~Ο~ (rotational strengths +14 Γ 10^β40^ and β32 Γ 10^β40^ esu^2^. cm^2^) plus a large nonβGaussian (βhelixβ) band with ampplitude β25,000Β° at 201 nm. These data appear to be in reasonably good accord with recent calculations.
Measurements of the absorption, linear dichroism and circular dichroism of polyproline I and II are also reported and are resolved into their component bands. Polyproline I is in good accord with exciton theory, whereas polyproline II remains unsatisfactory.
π SIMILAR VOLUMES
## Abstract For Abstract see ChemInform Abstract in Full Text.
## Abstract Circular dichroism spectra for acidβsoluble calfskin collagen, gelatin, and poly(proline) II in solution have been extended into the vacuum ultraviolet region. The extended spectrum of gelatin reveals that the circular dichroism of this unordered polymer is more closely related to the s