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dc.contributor.authorMorin, Trevor J.
dc.contributor.authorKobertz, William R.
dc.date2022-08-11T08:08:52.000
dc.date.accessioned2022-08-23T16:10:35Z
dc.date.available2022-08-23T16:10:35Z
dc.date.issued2008-06-11
dc.date.submitted2009-02-24
dc.identifier.citationJ Biol Chem. 2008 Sep 12;283(37):25105-9. Epub 2008 Jun 9. <a href="http://dx.doi.org/10.1074/jbc.R800033200">Link to article on publisher's site</a>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.R800033200
dc.identifier.pmid18541528
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32966
dc.description.abstractVoltage-gated K+ channels are dynamic macromolecular machines that open and close in response to changes in membrane potential. These multisubunit membrane-embedded proteins are responsible for governing neuronal excitability, maintaining cardiac rhythmicity, and regulating epithelial electrolyte homeostasis. High resolution crystal structures have provided snapshots of K+ channels caught in different states with incriminating molecular detail. Nonetheless, the connection between these static images and the specific trajectories of K+ channel movements is still being resolved by biochemical experimentation. Electrophysiological recordings in the presence of chemical modifying reagents have been a staple in ion channel structure/function studies during both the pre- and post-crystal structure eras. Small molecule tethering agents (chemoselective electrophiles linked to ligands) have proven to be particularly useful tools for defining the architecture and motions of K+ channels. This Minireview examines the synthesis and utilization of chemical tethering agents to probe and manipulate the assembly, structure, function, and molecular movements of voltage-gated K+ channel protein complexes.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=18541528&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1074/jbc.R800033200
dc.subjectAnimals; Biochemistry; Crystallography, X-Ray; Cysteine; Electrophysiology; Humans; Ion Channel Gating; Ligands; Membrane Potentials; Models, Biological; Models, Chemical; Molecular Conformation; Neurons; Potassium Channels, Voltage-Gated; Protein Conformation
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleTethering chemistry and K+ channels
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume283
dc.source.issue37
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1517
dc.identifier.contextkey738110
html.description.abstract<p>Voltage-gated K+ channels are dynamic macromolecular machines that open and close in response to changes in membrane potential. These multisubunit membrane-embedded proteins are responsible for governing neuronal excitability, maintaining cardiac rhythmicity, and regulating epithelial electrolyte homeostasis. High resolution crystal structures have provided snapshots of K+ channels caught in different states with incriminating molecular detail. Nonetheless, the connection between these static images and the specific trajectories of K+ channel movements is still being resolved by biochemical experimentation. Electrophysiological recordings in the presence of chemical modifying reagents have been a staple in ion channel structure/function studies during both the pre- and post-crystal structure eras. Small molecule tethering agents (chemoselective electrophiles linked to ligands) have proven to be particularly useful tools for defining the architecture and motions of K+ channels. This Minireview examines the synthesis and utilization of chemical tethering agents to probe and manipulate the assembly, structure, function, and molecular movements of voltage-gated K+ channel protein complexes.</p>
dc.identifier.submissionpathgsbs_sp/1517
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages25105-9


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