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Conformational change of poly(L-lysine) and poly(L-ornithine) and cooperative binding of sodium alkanesulfonate surfactants with different chain length

✍ Scribed by K. Hayakawa; H. Murata; I. Satake

Book ID
105184737
Publisher
Springer
Year
1990
Weight
638 KB
Volume
268
Category
Article
ISSN
0340-255X

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## Abstract The binding isotherms of sodium decyl sulfate to poly(L‐ornithine), poly(D,L‐ornithine), and poly(L‐lysine) at neutral pH were determined potentiometrically. The nature of a highly cooperative binding in all three cases suggests a micelle‐like clustering of the surfactant ions onto the

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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.