Protein Structure and Ion Binding in Potassium Selective Channels

dc.contributor.advisorJiang, Youxing, Ph.D.
dc.contributor.authorSauer, David Bryant
dc.date.accessioned2013-01-17T16:18:48Z
dc.date.accessioned2014-02-19T22:03:43Z
dc.date.available2013-01-17T16:18:48Z
dc.date.available2014-02-19T22:03:43Z
dc.date.issued2013-01-17
dc.description.abstractPotassium channels play a central role in a number of biological processes, most classically the action potential of excitable cells in multicellular organisms. These channels are defined by their selective conduction of potassium to the exclusion of other monovalent ions as governed by a common sequence and structural motif, the selectivity filter. This structure, made of backbone carbonyls and threonine side chains, directly coordinates the ions as they diffuse through the channel and appears central to this sub-angstrom discrimination between cations. Utilizing the non-selective Sodium and Potassium conducting channel (NaK) as a structural scaffold the mechanisms of both ion selectivity and formation of this selective structure are examined.en_US
dc.identifier.other841563990
dc.identifier.urihttp://hdl.handle.net/2152.5/1262
dc.subjectSodium-Potassium-Exchanging ATPase
dc.subjectPotassium
dc.subjectModels, Molecular
dc.titleProtein Structure and Ion Binding in Potassium Selective Channelsen_US
dc.typeThesisen_US
thesis.date.available2014-12-20
thesis.degree.disciplineMolecular Biophysics
thesis.degree.grantorGraduate School of Biomedical Sciences
thesis.degree.levelPh.D.
thesis.degree.nameDoctor of Philosophy

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