ku, Tokyo, J a p a n 104 ## Synopsis A I3C-nmr study of the salt-induced helix-coil transition of the basic polypeptides poly(L-lysine) [(Lys),], poly(i-arginine) [(Arg),], and poly(i-ornithine) [(Orn),] was performed to serve as a reference of the helical portion of histones and other proteins.
Conformational changes induced in ionized poly(L-arginine) and poly(L-histidine) by sodium dodecyl sulfate
✍ Scribed by Robert W. McCord; Ernest W. Blakeney Jr.; Wayne L. Mattice
- Book ID
- 102760599
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1977
- Tongue
- English
- Weight
- 532 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Circular dichroism spectra have been obtained for cationic poly(L‐arginine) and poly(L‐histidine) in aqueous solutions containing varying amounts of sodium dodecyl sulfate. The detergent induces a disorder‐order transition in both polypeptides. In each case the transition is cooperative and occurs when the ratio of detergent to amino acid residue is near unity. The ordered structure formed by poly(L‐arginine) is readily identifiable as an α helix. Poly(L‐histidine) appears to form a β structure in which the 211‐nm electronic absorption band of the imidazole group exhibits significant rotatory strength.
📜 SIMILAR VOLUMES
## Abstract The conformational phase diagram of poly(L‐lysine) (4.6 × 10^−4^ __M__, residue) in sodium dodecyl sulfate (1.6 × 10^−2^ __M__) solution was constructed from circular dichroism results at various temperatures and pH's. Poly(L‐lysine)–sodium dodecyl sulfate complexes undergo a β–helix tr
Organic solvent-induced coil + helix conformational change of poly(sodium L-glutamate (NaPLG) and poly(cesium L-glutamate) (CsPLG) in solution in aqueous mixed solvents have been studied at 25°C. H e a t s of dilution of NaPLG in the water-dioxane pair have been measured as a function of polymer con
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