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dc.creatorLi, Yunxiang
dc.date.accessioned2018-05-30T15:29:24Z
dc.date.available2018-05-30T15:29:24Z
dc.date.created2016-05
dc.date.issued2016-05
dc.date.submittedMay 2016
dc.identifier.urihttp://hdl.handle.net/2346/73738
dc.description.abstractATP synthase serves as a molecular engine, coupling ATP catalysis and proton translocation. To achieve this function, interactions between β and γ subunits are essential. In this study, the γ subunit was fixed at two signature angles, the ATP waiting dwell and the catalytic dwell. We found that the nucleotide binding patterns in these two time frames were greatly different; three catalytic sites were occupied at the catalytic dwell, meanwhile only two were occupied at the ATP waiting dwell. These observations further confirm that nucleotide binding affinity and conformation alternation of the catalytic sites are dependent on the rotational angle of the γ subunit. In addition, two segments of the γ subunit, γ5-15 and γ256-265, were further investigated with alanine replacement; the results revealed that the helical backbones, but not individual amino acid side chains, play important roles in determination of nucleotide binding affinity. Finally, γC87K mutation was identified to uncouple the ATP catalysis and proton translocation due to its positive charge, and a secondary γR242C/S mutation was found capable to suppress this uncoupling phenotype. More pieces of evidence suggest that γC87 could interact with both the C-terminus of γ and the βDELSEED motif.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.subjectATP synthase
dc.subjectNucleotide binding
dc.subjectEnergy coupling
dc.titleInteractions between β and γ subunits of ATP synthase are critical in nucleotide binding and energy coupling
dc.typeDissertation
dc.date.updated2018-05-30T15:29:25Z
dc.type.materialtext
thesis.degree.nameDoctor of Philosophy
thesis.degree.levelDoctoral
thesis.degree.disciplineChemistry
thesis.degree.grantorTexas Tech University
thesis.degree.departmentChemistry and Biochemistry
dc.contributor.committeeMemberParé, Paul W.
dc.contributor.committeeMemberLatham, Michael P.
dc.contributor.committeeChairWeber, Joachim
dc.rights.availabilityRestricted until 2021-05.
local.embargo.terms2021-05-01
local.embargo.lift2021-05-01


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