351 00 Padova, Ilaly synopsis Circular Dichroism measurements have been carried out on poly-L-lysine (PLL) and on random copolymers of lysine and phenylalanine a t various pH values and in the presence of different amounts of NaClOr. The results indicate that either the homopolymer or the copolymers
Nmr studies on complex formation of poly(L-lysine HBr) with carbonate ion in aqueous solution
β Scribed by Kinji Kakiuchi; Hideo Akutsu
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 769 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Dimer formation of poly(L-lysine HBr) in carbonate buffer a t pD 10.5 was reported in our previous paper [Biopolymers (1981) 20,345-3571. The mechanism of the dimer formation was investigated employing carbon-13 and proton nmr. pD dependence of the 13CC-nmr spectrum of poly(L-lysine HBr) in the presence of carbonate ion clearly shows that a complex formation between the COZ-ion and protonated r-amino group is involved in the stabilization of the dimer form. The lifetime of the complex is longer than s. A stoichiometric evaluation suggests that C0:-bridges two lysyl side chains. A molecular model of the dimer form designated as a single antiparallel ,&ribbon was proposed and discussed in the light of hydrodynamic and ir spectroscopic properties reported earlier. Concentration change experiments indicate that C0:binds not only to the dimer form, but also to the monomer form (a-helix). The role of the carbonate ion in the dimer formation is inferred as stabilization of the single antiparallel @-ribbon as an intermediate structure in the conversion between the a-helix and @-sheet. The a-CH proton signal of the lysine residue located in the ordered structure (a-helix and p-form) was observed to be separate from that in the random-coil region.
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