Studies of the structure and function of Mms6, a bacterial protein that promotes the formation of magnetic nanoparticles

dc.contributor.advisor Marit Nilsen-hamilton
dc.contributor.author Wang, Lijun
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2018-08-11T16:52:09.000
dc.date.accessioned 2020-06-30T02:39:48Z
dc.date.available 2020-06-30T02:39:48Z
dc.date.copyright Sat Jan 01 00:00:00 UTC 2011
dc.date.embargo 2013-06-05
dc.date.issued 2011-01-01
dc.description.abstract <p>Many highly ordered mineralized structures are created by living organisms that are often hierarchical in structure with fundamental structural elements at nanometer scales. The ability to fabricate such fundamental structures independently of these organisms could open many new and exciting opportunities in nanotechnology. In those cases for which there is some understanding of the biological mechanisms involved in biomineralization, proteins have been found responsible for forming the mineral structures. But, the mechanisms by which mineralization proteins function are poorly understood. Here we discuss our studies of the magnetotactic bacterial protein, Mms6, which promotes the formation in vitro of highly paramagnetic nanocrystals. Mms6 has two phases of iron binding, the first is very high affinity and the second is low affinity and cooperative with respect to iron. Our results provide evidence for a model for the mechanism of action of Mms6 in which a conformational change driven by a high affinity iron binding site in the C-terminal domain initiates a coordinated structural change involving multiple proteins to form a surface that can initiate the packing of iron into a crystal lattice. The small starting crystals might then fuse to produce larger nanoparticles as the protein islands move in a fluid hydrophobic environment of a membrane or micelles.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/etd/12014/
dc.identifier.articleid 3025
dc.identifier.contextkey 2808223
dc.identifier.doi https://doi.org/10.31274/etd-180810-1997
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath etd/12014
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/26217
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/etd/12014/WANG_iastate_0097E_11790.pdf|||Fri Jan 14 19:10:58 UTC 2022
dc.subject.disciplines Biochemistry, Biophysics, and Structural Biology
dc.title Studies of the structure and function of Mms6, a bacterial protein that promotes the formation of magnetic nanoparticles
dc.type article
dc.type.genre dissertation
dspace.entity.type Publication
relation.isOrgUnitOfPublication faf0a6cb-16ca-421c-8f48-9fbbd7bc3747
thesis.degree.level dissertation
thesis.degree.name Doctor of Philosophy
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