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
Polypeptide models of collagen: Properties of (Pro-Pro-βAla)n
✍ Scribed by Rajendra S. Bhatnagar; Rao S. Rapaka
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 335 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
We have synthesized (Pro-Pro-BAla), as a model for collagen. The synthetic polytripeptide, mol wt 6.500, exhibits a large negative optical rotation with a very strong negative Cotton effect centered a t 216 nm. The optical rotatory dispersion of (Pro-Pro-BAla), followed a single-term Drude equation and the X, was 19.5 nm. The rotation decreased markedly on heating with the midpoint of the broad transition a t 55°C. Preliminary studies also showed loss of structure in guadinine HCI. The circular dichroism spectrum of the polymer exhibited a deep trough a t 190 nm. The marked similarities of solution properties of (Pro-Pro-BAla), to (Pro-Pro-Gly), suggest that p-alanine can replace glycine in generating collagen-like helix in solution.
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## Abstract The conformation of (Pro‐Gly‐Phe)~__n__~ in trifluoroethanol was investigated using CD, nmr and ir techniques. After making appropriate correction for the contribution of the phenylalanine chromophore to the observed CD spectra of the polytripeptide at several temperatures, it is found
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.
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
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