The synthesis of the tripeptide polymers (Pro-Gly-Pro) n, (Pro-Pro-Gly) n, and (Gly-Pro-Pro),, is described, with particular attention to procedures which favor the efficient insertion of radioactive proline in either of the two proline positions 'X" or "Yr in the internal sequence, Gly-X-Y. By our
Synthesis of polytripeptide (pro-ser-gly)n, modeling the collagen type of structure
โ Scribed by V. A. Shibnev; Sh. Kh. Khalikov; M. P. Finogenova; K. T. Poroshin
- Book ID
- 112422938
- Publisher
- Springer
- Year
- 1970
- Tongue
- English
- Weight
- 236 KB
- Volume
- 19
- Category
- Article
- ISSN
- 1573-9171
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๐ SIMILAR VOLUMES
## Synopsis Conformational analysis of triple helices of a type of collagen was performed with typical collagen tripeptide sequences based on Gly-Pro-Ala, Gly-Ala-Hyp, and Gly-Ala-Ala. During energy minimization, the possibility of continual deformation of the pyrrolidine cycle was taken into acco
Our studies on the solution conformation of (Gly-Pro-Sar), and (Gly-Sar-Pro), synthesized as polypeptide models for collagen are reported. It is found that, while (Gly-Pro-Sar), exists in ordered triple-helical conformation, (Gly-Sar-Pro), remains as a disordered random coil in water. Addition of ce
On page 713, in Figure 4, the number at the top of the scale of the y-axis should read 0.0 rather than 2.0.