The crystal structure of despentapeptide insulin, a monomeric insulin, has been refined at 1.3 A spacing and subsequently used to predict and model the organization in the insulin fibril. The model makes use of the contacts in the densely packed despentapeptide insulin crystal, and takes into accoun
Unit fibril models derived from the molecular topography of collagen
✍ Scribed by Jere P. Segrest; Leon W. Cunningham
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 560 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The geometrical properties of collagen molecules place certain restrictions on possible three‐dimensional packing models. With certain reasonable assumptions involving the macromolecular structure of collagen, a model for the surface topography of the monomeric unit is developed and two possible models for molecular packing, one hexagonal and the other non‐hexagonal, are inferred. The non‐hexagonal packing model is identical to the pentagonal unit fibril first postulated by J. W. Smith on different grounds, while the hexagonal model is one of three previously suggested by us on more general assumptions. The two models are compared to available data on collagen packing, and the bulk of the evidence would seem to favor the pentagonal model.
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