Folded β-turns and collagenlike conformations of -Gly-Pro- and -Pro-Gly-sequences in synthetic polytripeptides
✍ Scribed by A. M. Tamburro; V. Guantieri
- Book ID
- 101720623
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1984
- Tongue
- English
- Weight
- 204 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3525
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📜 SIMILAR VOLUMES
Measurements of the molecular weight of (Pro-Pro-Gly), and (Pro-Pro-Gly),(Ala-Pro-Gly),(Pro-Pro-Gly),, which were synthesized by the solid-phase method, revealed that they formed a trimer in an aqueous solution, and dissociated into single-stranded chains on warming. Accompanying the transition, a l
## Abstract IR vibrational CD (VCD) has been observed for the cyclic pentapeptide __cyclo__‐(‐Gly‐Pro‐Gly‐D ‐Ala‐Pro‐) in solution in CDBr~3~. The observed VCD spectra do not resemble the VCD features of any of the previously reported peptide secondary structures, such as α‐helical, “random coil,”
## 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