CHAIN CONFORMATION IN THE COLLAGEN MOLECULE
CHAIN CONFORMATION IN THE COLLAGEN MOLECULE
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DOI：
10.1016/0022-2836(79)90507-2
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发表时间：
1979-01-01
影响因子：
5.6
通讯作者：
SUZUKI, E
中科院分区：
文献类型：
--
作者：
FRASER, RDB;MACRAE, TP;SUZUKI, E
从伸展的袋鼠尾腱收集定量X射线衍射数据，并用于测试胶原蛋白分子中多肽链构象的模型。分子螺旋的单位扭转的大小为107.1 °。.+-. 0.6 °，这接近于3圈10个单位的螺旋的预期值。强度数据被用来进行连接原子最小二乘模型的基础上提出的丰富和克里克2种可能的链间氢键键合方案的改进。没有立体化学上可接受的解决方案被发现的H键合方案的模型I，但立体化学上令人满意的解决方案被发现的方案的模型II，给出了晶体学R因子为0.272。
Quantitative X-ray diffraction data was collected from stretched kangaroo tail tendon and used to test models for the conformation of the polypeptide chains in the collagen molecule. The magnitude of the unit twist of the molecular helix was 107.1.degree. .+-. 0.6.degree., which is close to the value expected for a helix with 10 units in 3 turns. The intensity data were used to carry out a linked-atom least-squares refinement of models based on 2 possible interchain H bonding schemes suggested by Rich and Crick. No stereochemically acceptable solution was found for the H bonding scheme of model I but a stereochemically satisfactory solution was found for the scheme of model II which gave a crystallographic R factor of 0.272.