Raman spectroscopic studies of pig skin proteodermatan sulfate in H,O are indicative of a well defined secondary structure consisting of a-helical, P-turn, and possibly "random" structures. The above conclusion is surprisingly close to the secondary structure of the "core" protein of pig skin proteo
Raman spectroscopic study of arsenic speciation in aqueous solutions up to 275°C
✍ Scribed by Robert Gout; Gleb Pokrovski; Jacques Schott; Antoine Zwick
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 431 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0377-0486
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✦ Synopsis
Raman spectroscopic measurements were performed on solutions (0.02 O [ As ] O 5.2 mol kg-1) at As 2 O 3 -H 2 O temperatures from 20 to 275 ÄC. At 20 ÄC the spectrum of arsenic solutions of low concentration (0.02-0.5 mol kg-1) is the same over a wide range of pH (0-8). It only exhibits a polarized band at 700 cm-1 with a depolarized shoulder at 655 cm-1. These bands can be attributed to the pyramidal molecule
The spectrum of these As(OH) 3 0. solutions does not change signiÐcantly with increasing temperature. The only change consists in a small shift of the two bands towards low wavenumbers. In solutions of medium As concentration (1 mol kg-1), a broadening of the 700 cm-1 band towards low wavenumbers is observed. This can be explained by the formation of a non-dehydrated dimeric species which forms via hydrogen bridging bonds. At higher As concentrations (2-5.2 mol kg-1), a new band appears at 525 cm-1, the intensity of which increases with increasing As concentration and temperature. By comparison with the spectrum of fused arsenic oxide, this band can be attributed to AsÈOÈAs bonds. This suggests that polymeric species are present in concentrated As solutions. In the most concentrated solutions (4.1 and 5.2 mol kg-1), a new band occurs at 380 cm-1, which can be attributed to the symmetric stretching of the tetrahedron.
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