Three-dimensional model of adsorbed von Willebrand Factor using atomic force microscopy and mathematical morphology

Christopher Siedlecki, Brian J. Lestini, Steven J. Eppell, Kandice Kottke-Marchant, David Wilson, Roger E. Marchant

Research output: Chapter in Book/Report/Conference proceedingConference contribution

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 languageEnglish (US)
Title of host publicationTransactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium
Editors Anon
PublisherSoc for Biomaterials
Pages651
Number of pages1
Volume1
StatePublished - 1996
EventProceedings of the 1996 5th World Biomaterials Congress. Part 2 (of 2) - Toronto, Can
Duration: May 29 1996Jun 2 1996

Other

OtherProceedings of the 1996 5th World Biomaterials Congress. Part 2 (of 2)
CityToronto, Can
Period5/29/966/2/96

Fingerprint

Mathematical morphology
von Willebrand Factor
Atomic force microscopy
Proteins
Dimers
Contacts (fluid mechanics)
Conformations
Imaging techniques
Fluids

All Science Journal Classification (ASJC) codes

  • Materials Science(all)

Cite this

Siedlecki, C., Lestini, B. J., Eppell, S. J., Kottke-Marchant, K., Wilson, D., & Marchant, R. E. (1996). Three-dimensional model of adsorbed von Willebrand Factor using atomic force microscopy and mathematical morphology. In Anon (Ed.), Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium (Vol. 1, pp. 651). Soc for Biomaterials.
Siedlecki, Christopher ; Lestini, Brian J. ; Eppell, Steven J. ; Kottke-Marchant, Kandice ; Wilson, David ; Marchant, Roger E. / Three-dimensional model of adsorbed von Willebrand Factor using atomic force microscopy and mathematical morphology. Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium. editor / Anon. Vol. 1 Soc for Biomaterials, 1996. pp. 651
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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.",
author = "Christopher Siedlecki and Lestini, {Brian J.} and Eppell, {Steven J.} and Kandice Kottke-Marchant and David Wilson and Marchant, {Roger E.}",
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Siedlecki, C, Lestini, BJ, Eppell, SJ, Kottke-Marchant, K, Wilson, D & Marchant, RE 1996, Three-dimensional model of adsorbed von Willebrand Factor using atomic force microscopy and mathematical morphology. in Anon (ed.), Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium. vol. 1, Soc for Biomaterials, pp. 651, Proceedings of the 1996 5th World Biomaterials Congress. Part 2 (of 2), Toronto, Can, 5/29/96.

Three-dimensional model of adsorbed von Willebrand Factor using atomic force microscopy and mathematical morphology. / Siedlecki, Christopher; Lestini, Brian J.; Eppell, Steven J.; Kottke-Marchant, Kandice; Wilson, David; Marchant, Roger E.

Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium. ed. / Anon. Vol. 1 Soc for Biomaterials, 1996. p. 651.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

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AB - 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.

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Siedlecki C, Lestini BJ, Eppell SJ, Kottke-Marchant K, Wilson D, Marchant RE. Three-dimensional model of adsorbed von Willebrand Factor using atomic force microscopy and mathematical morphology. In Anon, editor, Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the International Biomaterials Symposium. Vol. 1. Soc for Biomaterials. 1996. p. 651