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Exploring induced secondary structure and unmethylated DNA binding domains of methyl CpG binding protein 2 (MeCP2)

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dc.contributor.authorHite, Kristopher Charles, author
dc.contributor.authorHansen, Jeffrey C., advisor
dc.contributor.authorWoody, Robert W., committee member
dc.contributor.authorRoss, Eric D., committee member
dc.contributor.authorMykles, Donald L., committee member
dc.date.accessioned2007-01-03T05:00:15Z
dc.date.available2007-01-03T05:00:15Z
dc.date.issued2011
dc.description.abstractOur understanding of Methyl CpG binding protein 2 (MeCP2) structure and function has changed and expanded considerably over the last two decades. Mutations along the entirety of the human MeCP2 gene product lead to a disease state - Rett syndrome. The clinical connection of this protein has continued to drive intense research into the nature of MeCP2 structure and function. There is now considerable and corroborated evidence that proves MeCP2 is an archetypical intrinsically disordered protein acting as a global ATP independent chromatin architectural protein. The ubiquity of MeCP2 in vertebrate neuronal nuclei has only recently been realized and has focused my investigations. Results from my work demonstrate a clear relationship between predicted α-molecular recognition features and inducible α- helical structure. From these data I suggest that inducible α-helices and maintained intrinsic disorder participate in binding the pool the twenty reported MeCP2 binding partners. In addition to structural studies I have identified two non-specific unmethylated DNA binding domains unreported in the literature at the onset of my work. I have also shown that MeCP2 acquires some secondary structural stability when bound to DNA and relatively little additional stability when bound to methylated DNA. The results presented here improve the fine resolution functional understanding of MeCP2 by observing isolated fragments of MeCP2 using both structural and functional methods. This approach is significant in and of itself as, like the large disordered subset of all eukaryotic proteins, the full-length MeCP2 molecule has proven impossible to crystallize thus far. Therefore narrowing the amino acid residues responsible for DNA binding activity or any other measurable functionality in a solution state is valuable.
dc.format.mediumborn digital
dc.format.mediumdoctoral dissertations
dc.identifierHite_colostate_0053A_10647.pdf
dc.identifier.urihttp://hdl.handle.net/10217/46753
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.subjectcircular dichroism
dc.subjectcloning
dc.subjectgenetic disease
dc.subjectMeCP2
dc.subjectprotein chemistry
dc.subjectRett Syndrome
dc.titleExploring induced secondary structure and unmethylated DNA binding domains of methyl CpG binding protein 2 (MeCP2)
dc.typeText
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineBiochemistry and Molecular Biology
thesis.degree.grantorColorado State University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy (Ph.D.)

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