Comparative conformational studies of polypeptides containing a high percentage of proline
β Scribed by Helbecque, N.; Loucheux-Lefebvre, M. H.
- Book ID
- 126512427
- Publisher
- American Chemical Society
- Year
- 1981
- Tongue
- English
- Weight
- 460 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0024-9297
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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.
As proline plays an important role in biologically active peptides, many analogues of this residue have been developed to modulate the proportion of cis and trans conformers. A correlation between the pyrrolidine ring shape and structural properties of proline has been established. Diketopiperazine