Structural Characterization of Two-Component Signal Transduction Proteins and Calbindin D28k

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dc.contributor.advisor Dennis T. Brown, Committee Member en_US
dc.contributor.advisor William L. Miller, Committee Member en_US
dc.contributor.advisor Ronald A. Venters, Committee Member en_US
dc.contributor.advisor Charles H. Opperman, Committee Member en_US
dc.contributor.advisor John Cavanagh, Committee Chair en_US
dc.contributor.author Kojetin, Douglas John en_US
dc.date.accessioned 2010-04-02T19:04:40Z
dc.date.available 2010-04-02T19:04:40Z
dc.date.issued 2006-11-17 en_US
dc.identifier.other etd-10042005-224222 en_US
dc.identifier.uri http://www.lib.ncsu.edu/resolver/1840.16/4939
dc.description.abstract The studies described involve the structural analysis of proteins involved in signal transduction pathways. In the first study, the metal binding properties of the initiation of sporulation response regulator Spo0F was studied using a variety of biophysical and biochemical techniques. The experiments show that most of the divalent metals studied, including and Ca²⁺, Mg²⁺ and Mn²⁺, which display primarily 1:1 binding, allow for favorable conditions for phosphotransfer between Spo0F and its cognate kinase KinA. In contrast, Spo0F binds up to three Cu²⁺ ions and the presence of this metal does not allow for the phosphotransfer reaction to occur. In the second study, a comparative modeling study of the OmpR sub-family of response regulators from B. subtilis and E. coli was performed and used to suggest the possibility of sub-classes within this related domain family based on regions of the response regulator regulatory domain that is known to interact with cognate four-helix bundle HisKA/Hpt domains. In the third study, the structural refinement of the four-helix bundle LuxU phosphotransferase from V. harveyi is described using a combination of dipolar couplings and water-based explicit refinement. In the fourth and last study, the development of a solution structure of Ca²⁺-loaded calbindin D[subscript 28k], an EF-hand calcium binding protein, and the interaction between peptides derived from ran-binding protein M and myo-inositol monophosphatase are described. en_US
dc.rights I hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to NC State University or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report. en_US
dc.subject Spo0F en_US
dc.subject two-component signal transduction en_US
dc.subject OmpR sub-family en_US
dc.subject LuxU en_US
dc.subject calbindin D28k en_US
dc.subject response regulators en_US
dc.subject ef-hand en_US
dc.title Structural Characterization of Two-Component Signal Transduction Proteins and Calbindin D28k en_US
dc.degree.name PhD en_US
dc.degree.level dissertation en_US
dc.degree.discipline Biochemistry en_US


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