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dc.contributor.advisorManson, Michael D.
dc.creatorGraybeal, Dion F.
dc.date.accessioned2022-04-01T16:04:03Z
dc.date.available2022-04-01T16:04:03Z
dc.date.issued1990
dc.identifier.urihttps://hdl.handle.net/1969.1/CAPSTONE-LovelaceL_1986
dc.descriptionProgram year: 1989/1990en
dc.descriptionDigitized from print original stored in HDRen
dc.description.abstractBacteria swim through their environment, but not that much is known about the "motor" which propels them. In Escherichia coli, a bacteria found in human intestines, six to eight flagella(4) move the cell around so that it can travel to "favorable environments." Both MotA and MotB, which are found in the cytoplasmic membrane (2, 11), form integral parts of this "motor," but in E. coli, it is not known what other proteins work in the motor. The motor is important because it transforms the electrochemical potential energy of H⁺ ions into a physical force on the molecular level. My research has revealed that there is a protein that interacts with MotA.en
dc.format.extent23 pagesen
dc.format.mediumelectronicen
dc.format.mimetypeapplication/pdf
dc.subjectEscherichia colien
dc.subjectflagellaen
dc.subjectMotAen
dc.subjectMotBen
dc.subjectelectrochemical potential energyen
dc.titleIsolation of Genetic Second-Site Suppressor Mutations of the Mot genes in Escherichia coli to Determine the Function of the Mot proteinsen
dc.typeThesisen
thesis.degree.departmentBiologyen
thesis.degree.grantorUniversity Undergraduate Fellowen
thesis.degree.levelUndergraduateen
dc.type.materialtexten


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