CONFORMATIONAL STUDIES ON SEQUENTIAL POLYPEPTIDES.
β Scribed by Scatturin, A. ;Tamburro, A. M. ;Vidali, G. ;Bordignon, E.
- Book ID
- 115097166
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 487 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0367-8377
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## Abstract The conformation of three sequential copolypeptides, poly(LβtyrosylβLβlysine), poly(LβtyrosylβLβlysylβLβlysine), and poly[Lβtyrosylβ(Lβlysyl)~2~βLβlysine] have been studied by a variety of techniques, including CD, ir spectroscopy, analytical ultracentrifugation, and xβray diffraction.
The sequential polypeptides (L-Arg-X-Gly),, where X represents amino acid residues Ala, Val, and Leu, were prepared as models of argininerich histones to be used in studying their structure and their interactions with DNA. The polymerization was carried out on the pentachlorophenyl active esters of
The pyridoxal Schiff bases of the polypeptides poly(L-lysine), poly(L-ornithine), and poly(L-a,y-diaminobutyric acid) were prepared and investigated in water/methanol by CD spectra and equilibrium dialysis experiments. Only the poly(L-a,?-diaminobutyric acid) derivative is characterized by a relevan