## Abstract The Raman and infrared spectra of poly(L‐lysine) and poly(DL‐lysine) in solution are reported and the effects of various salts are investigated. The results demonstrate that α‐helix formation in solution is induced by specific salts and the spectral data support the hypothesis of region
Laser Raman studies of conformational variations of poly-L-lysine
✍ Scribed by Tain-Jen Yu; Joseph L. Lippert; Warner L. Peticolas
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 690 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The frequencies and intensities of the laser Raman spectra of poly‐L‐lysine (PLL) have been observed in the following studies: (1) the thermally induced α‐to‐β transition which occurs with increasing temperature at high pH; (2) the ionized form to α transition at 10°C by increasing pH; and (3) the ionized form to α transition by ionic strength at low pH.
The frequency‐dependent bands which have been observed are the amide I (in H~2~O), amide I′ (in D~2~O), amide III, and C–C stretch. It has been found possible to assign an unique set of frequencies and intensities to each conformation of PLL of α, β, and ionized form. In this way the nature of the conformations intermediate in the transitions can be determined. The frequencies of the amide III and amide III′ are very weak in the α‐helix and somewhat higher than usual in the β form. Hence it appears the amide III and amide III′ bands may differ from one type of polypeptide to another with the same backbone conformation.
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## Abstract The Raman spectra of poly‐L‐lysine hydrochloride and poly‐ϵ‐carbobenzoxy‐L‐lysine in the solid state have been obtained and are consistent with the presence of an α‐helical structure. The Raman spectrum of poly‐L‐lysine in aqueous solution suggests the presence of random coil structures
## Abstract Complexes of polyribocytidylic acid and polyriboadenylic acid with poly(L‐lysine) and poly(L‐arginine) were studied by Raman spectroscopy. The backbones of both polynucleotides are distorted by poly(L‐arginine). On the other hand, poly(L‐lysine) could distort the backbone of polyriboade
## Abstract The Raman spectra of poly(L‐lysine) with various structures, ionized poly(L‐glutamic acid), and deuterated __N__‐methylacetamides have been observed using visible and the 257.3‐nm laser lines as the light source. Most of the Raman bands with significantly enhanced intensities in the uv‐
The effect of the number of methylene groups in the side chains on the conformation of polypeptides is assessed for three poly(L-lysine) homologs with R = -(CHz),,NHz. Circular dichroism studies show a pH-induced helix-coil transition in 0.05 M KCl with midpoints a t 9.6, 9.0, and 8.7 for n = 5, 6,
The binding of the methylmercury cation CH3Hg+ by poly(L-glutamic acid) (PGA) and by poly(i-lysine) (PLL) has been investigated by b a n spectroscopy. Coordination on the side-chain COO-and NH; groups of these polypeptides gave characteristic ligand-Hg stretching modes at ca. 505 and 450 cm-', respe