Mechanical properties of complex biological systems using AFM-based force spectroscopy

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Mechanical properties of complex biological systems using AFM-based force spectroscopy

Please use this identifier to cite or link to this item: http://hdl.handle.net/10355/4191

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dc.contributor.author Graham, John Stephen, 1965- en
dc.date.accessioned 2010-01-06T21:20:27Z
dc.date.available 2010-01-06T21:20:27Z
dc.date.issued 2005 en_US
dc.date.submitted 2005 Fall en
dc.identifier.other GrahamJ-121205-D3743 en_US
dc.identifier.uri http://hdl.handle.net/10355/4191
dc.description The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. en_US
dc.description Title from title screen of research.pdf file (viewed on October 18, 2007) en_US
dc.description Vita. en_US
dc.description Includes bibliographical references. en_US
dc.description Thesis (Ph. D.) University of Missouri-Columbia 2005. en_US
dc.description Dissertations, Academic -- University of Missouri--Columbia -- Physics. en_US
dc.description.abstract An atomic force microscope (AFM) was designed and built to study the mechanical properties of small collagen fibrils and the plasma membrane of living cells. Collagen is a major component of bone, skin and connective tissues, and is abundant in the extracellular matrix (ECM). Because of its abundance, an understanding of how disease affects collagen mechanics is crucial in disease prevention efforts. Two levels of type I collagen structure were investigated, subfibrils (on the order of 1 [mu] m in length) and longer fibrils. Comparisons were made between measurements of wild-type (wt) collagen and collagen from the mouse model of osteogenesis imperfecta (OI). Significant differences between OI and wt collagen were observed, primarily that intermolecular bonds in OI collagen fibrils are weaker than in wt, or not ruptured, as in the case of OI subfibrils. As cells interact with collagen in the ECM, the mechanical properties of the plasma membrane are also of great interest. Membrane tethers were extracted from living cells under varied conditions in order to assess the contributions of membrane-associated macromolecules such as the actin cytoskeleton and the glycocalyx, as well as intracellular signaling processes triggered by thapsigargin. Tether extraction force was found to be sensitive to all of these altered conditions, suggesting that tether extraction may be used to monitor various cellular processes. en_US
dc.language.iso en_US en_US
dc.publisher University of Missouri--Columbia en_US
dc.relation.ispartof 2005 Freely available dissertations (MU) en_US
dc.subject.lcsh Atomic force microscopy en_US
dc.subject.lcsh Osteogenesis imperfecta en_US
dc.subject.lcsh Cell membranes en_US
dc.subject.lcsh Extracellular matrix proteins en_US
dc.subject.lcsh Collage en_US
dc.title Mechanical properties of complex biological systems using AFM-based force spectroscopy en_US
dc.type Thesis en_US
thesis.degree.discipline Physics en_US
thesis.degree.grantor University of Missouri--Columbia en_US
thesis.degree.name Ph. D. en_US
thesis.degree.level Doctoral en_US
dc.identifier.merlin .b60595565 en_US
dc.identifier.oclc 174966906 en_US
dc.relation.ispartofcommunity University of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2005 Dissertations


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