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dc.contributor.advisorTanner, John J.eng
dc.contributor.authorOu, Zhonghuieng
dc.date.issued2006eng
dc.date.submitted2006 Springeng
dc.descriptionThe 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.eng
dc.descriptionTitle from title screen of research.pdf file (viewed on April 17, 2009)eng
dc.descriptionIncludes bibliographical references.eng
dc.descriptionThesis (M.S.) University of Missouri-Columbia 2006.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Biochemistry (Agriculture).eng
dc.description.abstractDNA-1 and 11F8 are anti-ss DNA antibodies derived from autoimmune lupus-prone mice. They are very similar to each other in terms of CDR sequence and preference for binding T-rich ss DNA. G1-17 is an oligonucleotide identified by in vitro selection experiments and binds with high affinity and specificity to Fab 11F8. G5-14 is a synthetic oligonucleotide with the tennucleotide sequence identical to the stem-loop portion above the bulge of G1-17. The 1.95 A ̊resolution DNA-1/G5-14 structure shows that the two DNA strands dimerize to form a double stranded DNA dumbbell and have a large conformational change including the breaking and reformation of hydrogen bonds. The most striking feature of the Fab/DNA interactions is the use of extensive [pi-pi] stacking of the DNA bases and the protein side chains. These results provide insights into the specific recognition model of anti-DNA Abs and the potential challenges in structure based drug design to treat autoimmune diseases. The second part of this thesis describes purification and crystallization of Haemophilus influenzae class C acid phosphatise P4, and acquisition of a 1.7 Å ̊resolution native X-ray diffraction data set. The space group of the crystals is P4₂2₁2 with a = 65.6, c = 101.4 A ̊one protein molecule per asymmetric unit and 37 % solvent content. This is the first report of crystallization of a class C acid phosphatase.eng
dc.identifier.merlinb66787476eng
dc.identifier.oclc318650809eng
dc.identifier.urihttps://hdl.handle.net/10355/4621
dc.identifier.urihttps://doi.org/10.32469/10355/4621eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcommunityUniversity of Missouri--Columbia. Graduate School. Theses and Dissertationseng
dc.sourceSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subject.lcshDNAeng
dc.subject.lcshCrystallizationeng
dc.subject.lcshAcid phosphataseeng
dc.subject.lcshHaemophilus influenzaeeng
dc.titleStructure of an antigen-binding fragment bound to stem-loop DNA and crystallization of recombinant haemophilus influenzae e(P4) acid phosphataseeng
dc.typeThesiseng
thesis.degree.disciplineBiochemistry (Agriculture) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelMasterseng
thesis.degree.nameM.S.eng


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