𝔖 Bobbio Scriptorium
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Electronic structures of collagen model polymers: (Gly-Pro)n, (Gly-Hyp)n, (Ala-Pro)n, (Ala-Hyp)n, (Gly-Pro-Gly)n, (Gly-Hyp-Gly)n, (Gly-Pro-Pro)n, and (Gly-Pro-Hyp)n

✍ Scribed by Masaru Ohsaku; Junya Izumi; Akiar Imamura

Book ID
119069927
Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
596 KB
Volume
6
Category
Article
ISSN
0141-8130

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📜 SIMILAR VOLUMES

Comprehensive conformational analysis of
Comprehensive conformational analysis of (Gly-Pro-Pro)n and (Gly-Pro-Hyp)n related to collagen
✍ Vladimir G. Tumanyan; Natalia G. Esipova 📂 Article 📅 1982 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 959 KB

## Abstract A complete analysis of all possible conformations with correct hydrogen bonds of the collagen II type was performed on the basis of developed simultaneous equations. Using a unimodal search (by varying Ψ^3^), the energetically favorable structure was obtained. No other energetically sat

Conformational analysis of polytripeptid
Conformational analysis of polytripeptides (Gly-Pro-Ala)n, (Gly-Ala-Hyp)n, and (Gly-Ala-Ala)n in connection with the problem of collagen structure
✍ V. G. Tumanyan; R. A. Abagyan; N. G. Esipova 📂 Article 📅 1984 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 665 KB

## 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

Conformational change of the triple-heli
Conformational change of the triple-helical structure. II. Conformation of (Pro-Pro-Gly)n and (Pro-Pro-Gly)n(Ala-Pro-Gly)m(Pro-Pro-Gly)n in an aqueous solution
✍ Kazuo Sutoh; Haruhiko Noda 📂 Article 📅 1974 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 678 KB

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

Synthesis of poly(Pro–Hyp–Gly)n by direc
Synthesis of poly(Pro–Hyp–Gly)n by direct polycondensation of (Pro–Hyp–Gly)n, where n = 1, 5, and 10, and stability of the triple-helical structure
✍ Takahiro Kishimoto; Yasushi Morihara; Michinori Osanai; Shin-ichi Ogata; Masanob 📂 Article 📅 2005 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 566 KB

## Abstract Pro–Hyp–Gly is a characteristic amino acid sequence found in fibrous collagens, and (Pro–Hyp–Gly)~10~, which has been widely used as a collagen‐model peptide, forms a stable triple‐helical structure. Here, we synthesized polypeptides consisting of the Pro–Hyp–Gly sequence by direct poly