Abstract
The 3-dimensional structure of protein was investigated as well as the effect of conformational changes in the von Willebrand Factor (vWF) on protein function. The effects of applied shear were studied using different atomic force microscopy (AFM) imaging models, while mathematical morphology was used to generate a model of an adsorbed vWG dimer and to predict AFM images. It was shown that submolecular three-dimensional resolution of vWF can be obtained in aqueous solutions using both contact mode and fluid-tapping mode. In the absence of applied shear, vWF adsorbs in a large globular conformation. Applied shear leads to the unraveling of the protein and exposure of the individual domains.
Original language | English (US) |
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Title of host publication | Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium |
Editors | Anon |
Publisher | Soc for Biomaterials |
Pages | 651 |
Number of pages | 1 |
Volume | 1 |
State | Published - 1996 |
Event | Proceedings of the 1996 5th World Biomaterials Congress. Part 2 (of 2) - Toronto, Can Duration: May 29 1996 → Jun 2 1996 |
Other
Other | Proceedings of the 1996 5th World Biomaterials Congress. Part 2 (of 2) |
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City | Toronto, Can |
Period | 5/29/96 → 6/2/96 |
All Science Journal Classification (ASJC) codes
- General Materials Science