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Conformational studies of cyclohexapeptide analogs of elastin sequences: Cyclo(Ala-Pro-Gly-Ala-Pro-Gly)

✍ Scribed by V. Renugopalakrishnan; H. Sugano; M. A. Khaled; R. S. Rapaka; D. W. Urry

Book ID
104579415
Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
457 KB
Volume
14
Category
Article
ISSN
0020-7608

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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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## 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

IR (vibrational) CD of peptide Ξ²-turns:
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✍ Herman R. Wyssbrod; Max Diem πŸ“‚ Article πŸ“… 1992 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 506 KB

## 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, β€œrandom coil,”