ISSN:
0006-3525
Schlagwort(e):
Chemistry
;
Polymer and Materials Science
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Chemie und Pharmazie
Notizen:
Conformational transitions of basic sequential polytripeptides (Lys-Ala-Leu)n, (Arg-Ala-Ala)n, (Arg-Leu-Ala)n, and (Arg-Ala-Leu)n, induced by elevated salt concentrations and/or temperatures in aqueous solutions, were investigated by CD, sedimentation equilibrium, and viscometry. The behavior of (Lys-Ala-Leu)n was compared with that of the sequential isomer (Lys-Leu-Ala)n, studied previously. It was found that both polypeptides are highly helical with a tendency to aggregate in high salt solutions. Although the hydrophobic interactions between Lys and Leu residues play an important role in both cases, the final effect on helix stabilization and aggregation is different. The Arg-containing polypeptides were found to assume the α-helical conformation. Compared to the Lys-containing polypeptides (Lys-Ala-Leu)n and (Lys-Leu-Ala)n, a very low tendency to aggregate was observed.
Zusätzliches Material:
6 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/bip.360281007
