Conformational change of poly(l-lysine) induced by lipid vesicles of dilauroylphosphatidic acid
โ Scribed by Kohsuke Fukushima; Yoshihiro Muraoka; Tohru Inoue; Ryosuke Shimozawa
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 673 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0301-4622
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๐ SIMILAR VOLUMES
## Abstract Transient electric birefringence measurements on poly(Lโlysine hydrobromide) in methanolโwater mixtures have been carried out at various solvent compositions in the vicinity of the helixโcoil transition region (from 87 to 98 vol % methanol). Anomalous birefringence transients were obser
Poly-L-lysine exists as an a-helix at high pH and a random coil at neutral pH. When the a-helix is heated above 27ะC, the macromolecule undergoes a conformational transition to a b-sheet. In this study, the stability of the secondary structure of poly-L-lysine in solutions subjected to shear flow, a
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.
## Abstract The conformational changes of polyโ__N__^ฮต^โglutarylโLโlysine (PGL) and polyโ__N__^ฮต^โsuccinylโLโlysine (PSL) in various salt solutions were studied by use of ORD and potentiometric titration measurements. The addition of alkali metal salts to the fully ionized PGL or PSL solution cause