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dc.contributor.author Runke, Gregory S. en_US
dc.date.accessioned 2007-06-01T19:24:25Z
dc.date.available 2007-06-01T19:24:25Z
dc.date.issued 2000-08-01T00:00:00Z en_US
dc.identifier.uri http://hdl.handle.net/1993/2417
dc.description.abstract Mitochondrial porin is a voltage-gated, anion-selective channel that facilitates the diffusion of small hydrophilic molecules across the mitochondrial outer membrane. The "glycine-leucine-lysine" (GLK) motif of porin is highly conserved among different species even though overall sequence similarity is quite low. The GLK motif is thought to be part of the ATP binding site for porin. ATP binding is known to alter ion selectivity of 'N. crassa ' porin. The GLK motif of 'N. crassa' porin was changed to GLE through site-directed mutagenesis. Cross-linking studies with 32P-ATP indicate that the GLE mutant was able to bind ATP while electrophysiological measurements indicate that the GLE mutant is able to form a pore in lipid bilayers with altered ion selectivity. Several versions of a B-barrel structural model have been proposed for mitochondrial porin. To further refine these models, a series of mutant versions of the porin of 'Neurospora crassa' were generated. (Abstract shortened by UMI.) en_US
dc.format.extent 4676374 bytes
dc.format.extent 184 bytes
dc.format.mimetype application/pdf
dc.format.mimetype text/plain
dc.language en en_US
dc.language.iso en_US
dc.rights info:eu-repo/semantics/openAccess
dc.title Functional and structural studies of mitochondrial porin en_US
dc.type info:eu-repo/semantics/masterThesis
dc.degree.discipline Microbiology en_US
dc.degree.level Master of Science (M.Sc.) en_US


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