Posted by lettsscience on September 15, 2012 · 6 Comments
In this post I continue my series on the omega current by discussing how a mutation that removes a charged group from the voltage-sensor domain (VSD) would be highly destabilizing and disruptive. The omega current is a leak current that passes through the VSD of mutated voltage-gated cation channels. In some cases, the mutated channels … Continue reading →
Filed under Biochemistry, Biophysics, Hv, Ion channels, Opinion, Review, Science, Voltage gating · Tagged with 6TM channels, gated ion channels, ion selectivity, molecular mechanism, omega current, omega pore, Opinion, protein architechture, protein structure function, S4 helix, voltage gating, voltage sensor domain, voltage-gated cation channels
Posted by lettsscience on August 20, 2012 · 4 Comments
In this post I will be continuing my series on the omega current. The omega current is a leak current that passes through the voltage-sensor domain (VSD) of mutated voltage-gated cation channels. Mutation of the VSD S4 helix can reveal a cryptic pore that allows ions (H+, Li+, K+, Rb+ and even guanidinium) to cross … Continue reading →
Filed under Biochemistry, Biophysics, Ion channels, Opinion, Physiology, Review, Science, Voltage gating · Tagged with 6TM channels, Benign familial neonatal epilepsy, channelopathy, hypkalemic periodic paralysis, ion channels, omega current, omega pore, Opinion, Peripheral nerve hyperexcitability, protein architechture, protein structure function, Review, S4 helix, science, voltage gating, voltage sensor domain, voltage-gated cation channels
Posted by lettsscience on June 20, 2012 · 1 Comment
In this post I will finish my series on alignments and homology models. Here, I will discuss three different biochemical studies of the voltage-gated proton channel (Hv) that help to delineate the boundaries of the S4 helix. First, I will discuss the structure of the coiled-coil, which limits where along the primary the sequence of … Continue reading →
Filed under Biochemistry, Hv, Ion channels, Review, Science, Voltage gating · Tagged with coiled-coil, gated ion channels, homology models, human voltage-gated proton channel, Hv, ion channels, molecular mechanism, Opinion, protein sequence, protein sequence alignments, protein structure function, S4 helix, science, voltage gating, voltage sensor domain, voltage-gated cation channels, voltage-gated proton channel
Standard ·
Posted by lettsscience on June 1, 2012 · 2 Comments
In this post, I will elaborate upon a statement I made in last week’s post. There, I discussed how important a proper alignment of the S4 helices in voltage sensor domains (VSDs) is for building accurate homology-based structural models of these domains. When discussing the potential alignments I stated that “since the different conformations of … Continue reading →
Filed under Biochemistry, Hv, Ion channels, Voltage gating · Tagged with gated ion channels, gating charge residues, human voltage-gated proton channel, Hv, ion channels, molecular mechanism, Opinion, protein sequence alignments, protein structure function, S4 helix, science, voltage gating, voltage sensor domain, voltage-gated cation channels, voltage-gated proton channel
LettsScience 