## Abstract Raman spectra in the region 1000–150 cm^−1^ were measured for copoly(D,L‐alanines) with the D‐residue contents, 3, 7, 10, and 20%, and compared with the spectrum of the α‐helical poly‐L‐alanine. The 532‐ and 378‐cm^−1^ peaks were assigned to the L‐residues with a right‐handed α‐helix‐li
Raman spectra of L-alanine oligomers
✍ Scribed by P. Sutton; J. L. Koenig
- Book ID
- 102762314
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1970
- Tongue
- English
- Weight
- 680 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The Raman spectra have been obtained of di‐, tri‐, tetra‐, penta‐, and hexa‐L‐alanine in the solid state. Raman spectra of the dimer and trimer in aqueous solution are also reported. The oligomers of alanine exist as zwitterions in the solid state and aqueous solution. Spectral differences between the dipeptide, and other oligomers arise primarily from the conformationally sensitive amide modes. The dipeptide exists as a nonplanar structure in the solid state and the other oligomere as β conformations. Comparison of Raman spectra of tri‐L‐alanine in the solid state and in aqueous solution suggests a conformational change to a random coil upon dissolution.
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