An X-ray study of the synthetic polypeptide (Pro-Pro-Gly) 10

A polypeptide, (Pro-Pro-Gly) 10, synthesized as a collagen model, gave a single crystal suitable for X-ray analysis with unit cell dimensions a = 26.9, b = 26.4, c = 100.4 A ̊ , and space group P2 12 12 1. The unit cell consists of four triple helices, whose locations are indicated on a tentative el...

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Published inJournal of molecular biology Vol. 72; no. 3; pp. 571,IN1,573 - 572,IN1,576
Main Authors Okuyama, Kenji, Tanaka, Nobuo, Ashida, Tamaichi, Kakudo, Masao, Sakakibaka, Shumpei, Kishida, Yasuo
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 30.12.1972
Subjects
Amino Acid Sequence
Collagen
Glycine
Molecular Conformation
Peptides
Proline
X-Ray Diffraction
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Summary:A polypeptide, (Pro-Pro-Gly) 10, synthesized as a collagen model, gave a single crystal suitable for X-ray analysis with unit cell dimensions a = 26.9, b = 26.4, c = 100.4 A ̊ , and space group P2 12 12 1. The unit cell consists of four triple helices, whose locations are indicated on a tentative electron-density projection along the fiber axis. The helical parameters obtained from the three-dimensional intensity distribution and Patterson maps are: major helix radius 2.8 Å; major helix pitch 60.24 Å; vertical distance (parallel to c axis) between residues 2.87 Å; number of residues in the repeat distance 21; and number of turns of minor helix in the repeat distance 7.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0022-2836
1089-8638
DOI:10.1016/0022-2836(72)90175-1