title: A three-state model for connexin37 gating kinetics.
abstract: The gating behavior of human connexin 37 (hCx37) is unaffected by the nature of the bathing monovalent (for Na, K, Rb). It is modified by [Mg] in the millimolar range. For fitting the kinetics, we propose a simple extension to three states of the canonical 2-state model of the hemichannel. The extra closed state allows for some immobilization of a hemichannel at high transjunctional voltages. The model is reasonably efficient at fitting data at various voltage protocols. Interpreting the fits of the data at different [Mg] is consistent with a binding site for Mg.
authors.affiliation: Department of Physiology and Biophysics, State University of New York at Stony Brook, Stony Brook, New York 11794-8661, USA.
authors.forename: S V
authors.initials: SV
authors.lastname: Ramanan
authors.forename: P R
authors.initials: PR
authors.lastname: Brink
authors.forename: K
authors.initials: K
authors.lastname: Varadaraj
authors.forename: E
authors.initials: E
authors.lastname: Peterson
authors.forename: K
authors.initials: K
authors.lastname: Schirrmacher
authors.forename: K
authors.initials: K
authors.lastname: Banach
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D017630:Connexins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004563:Electrochemistry; D006801:Humans; D066298:In Vitro Techniques; D015640:Ion Channel Gating / Q000187:drug effects; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008954:Models, Biological; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014162:Transfection; D014407:Tumor Cells, Cultured; D000097006:Gap Junction alpha-4 Protein
chemical_list: D017630:Connexins; D008274:Magnesium; D011994:Recombinant Proteins; D000097006:Gap Junction alpha-4 Protein