Viscosity and density of methanol/water mixtures at low temperatures

Viscosity and density are measured at low temperatures for three methanol/water mixtures. Viscosity is determined by a modified falling cylinder method or a calibrated viscometer. Density is determined by the volume of each mixture contained in a calibrated glass cell placed in a constant-temperature bath

The Polyamine Binding Site in Inward Rectifier K+ Channels

Strongly inwardly rectifying potassium channels exhibit potent and steeply voltage-dependent block by intracellular polyamines. To locate the polyamine binding site, we have examined the effects of polyamine blockade on the rate of MTSEA modification of cysteine residues strategically substituted in the pore of a strongly rectifying Kir channel (Kir6.2[N160D]). Spermine only protected cysteines substituted at a deep location in the pore, between the “rectification controller” residue (N160D in Kir6.2, D172 in Kir2.1) and the selectivity filter, against MTSEA modification. In contrast, blockade with a longer synthetic polyamine (CGC-11179) also protected cysteines substituted at sites closer to the cytoplasmic entrance of the channel. Modification of a cysteine at the entrance to the inner cavity (169C) was unaffected by either spermine or CGC-11179, and spermine was clearly “locked” into the inner cavity (i.e., exhibited a dramatically slower exit rate) following modification of this residue. These data provide physical constraints on the spermine binding site, demonstrating that spermine stably binds at a deep site beyond the “rectification controller” residue, near the extracellular entrance to the channel

The Polyamine Binding Site in Inward Rectifier K+ Channels

Strongly inwardly rectifying potassium channels exhibit potent and steeply voltage-dependent block by intracellular polyamines. To locate the polyamine binding site, we have examined the effects of polyamine blockade on the rate of MTSEA modification of cysteine residues strategically substituted in the pore of a strongly rectifying Kir channel (Kir6.2[N160D]). Spermine only protected cysteines substituted at a deep location in the pore, between the “rectification controller” residue (N160D in Kir6.2, D172 in Kir2.1) and the selectivity filter, against MTSEA modification. In contrast, blockade with a longer synthetic polyamine (CGC-11179) also protected cysteines substituted at sites closer to the cytoplasmic entrance of the channel. Modification of a cysteine at the entrance to the inner cavity (169C) was unaffected by either spermine or CGC-11179, and spermine was clearly “locked” into the inner cavity (i.e., exhibited a dramatically slower exit rate) following modification of this residue. These data provide physical constraints on the spermine binding site, demonstrating that spermine stably binds at a deep site beyond the “rectification controller” residue, near the extracellular entrance to the channel

Disorder-induced topological change of the superconducting gap structure in iron pnictides

In superconductors with unconventional pairing mechanisms, the energy gap in the excitation spectrum often has nodes, which allow quasiparticle excitations at low energies. In many cases, e.g. $d$-wave cuprate superconductors, the position and topology of nodes are imposed by the symmetry, and thus the presence of gapless excitations is protected against disorder. Here we report on the observation of distinct changes in the gap structure of iron-pnictide superconductors with increasing impurity scattering. By the successive introduction of nonmagnetic point defects into BaFe$_2$(As$_{1-x}$P$_x$)$_2$ crystals via electron irradiation, we find from the low-temperature penetration depth measurements that the nodal state changes to a nodeless state with fully gapped excitations. Moreover, under further irradiation the gapped state evolves into another gapless state, providing bulk evidence of unconventional sign-changing $s$-wave superconductivity. This demonstrates that the topology of the superconducting gap can be controlled by disorder, which is a strikingly unique feature of iron pnictides.Comment: 5 pages, 4 figure