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the u.s. policy in central asia and its impact on the colored revolutions in the region (the case study of tulip revolution in kyrgyzstan)
چکیده ندارد.
15 صفحه اولProton transport pathway in the ClC Cl-/H+ antiporter.
A fundamental question concerning the ClC Cl-/H+ antiporters is the nature of their proton transport (PT) pathway. We addressed this issue by using a novel computational methodology capable of describing the explicit PT dynamics in the ClC-ec1 protein. The main result is that the Glu203 residue delivers a proton from the intracellular solution to the core of ClC-ec1 via a rotation of its side c...
متن کاملIntracellular Proton Regulation of ClC-0
Some CLC proteins function as passive Cl(-) ion channels whereas others are secondary active chloride/proton antiporters. Voltage-dependent gating of the model Torpedo channel ClC-0 is modulated by intracellular and extracellular pH, possibly reflecting a mechanistic relationship with the chloride/proton coupling of CLC antiporters. We used inside-out patch clamp measurements and mutagenesis to...
متن کاملProton Sensing of CLC-0 Mutant E166D
CLC Cl- channels are homodimers in which each subunit has a proper pore and a (fast) gate. An additional slow gate acts on both pores. A conserved glutamate (E166 in CLC-0) is a major determinant of gating in CLC-0 and is crucially involved in Cl-/H+ antiport of CLC-ec1, a CLC of known structure. We constructed tandem dimers with one wild-type (WT) and one mutant subunit (E166A or E166D) to sho...
متن کاملIntracellular Proton-Transfer Mutants in a CLC Cl−/H+ Exchanger
CLC-ec1, a bacterial homologue of the CLC family's transporter subclass, catalyzes transmembrane exchange of Cl(-) and H(+). Mutational analysis based on the known structure reveals several key residues required for coupling H(+) to the stoichiometric countermovement of Cl(-). E148 (Glu(ex)) transfers protons between extracellular water and the protein interior, and E203 (Glu(in)) is thought to...
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ژورنال
عنوان ژورنال: The Journal of Physiology
سال: 2009
ISSN: 0022-3751
DOI: 10.1113/jphysiol.2009.169623