Modeling the ion channel structure of cecropin.

Atomic-scale computer models were developed for how cecropin peptides may assemble in membranes to form two types of ion channels. The models are based on experimental data and physiochemical principles. Initially, cecropin peptides, in a helix-bend-helix motif, were arranged as antiparallel dimers to position conserved residues of adjacent monomers in contact. The dimers were postulated to bind to the membrane with the NH2-terminal helices sunken into the head-group layer and the COOH-terminal helices spanning the hydrophobic core. This causes a thinning of the top lipid layer of the membrane. A collection of the membrane bound dimers were then used to form the type I channel structure, with the pore formed by the transmembrane COOH-terminal helices. Type I channels were then assembled into a hexagonal lattice to explain the large number of peptides that bind to the bacterium. A concerted conformational change of a type I channel leads to the larger type II channel, in which the pore is formed by the NH2-terminal helices. By having the dimers move together, the NH2-terminal helices are inserted into the hydrophobic core without having to desolvate the charged residues. It is also shown how this could bring lipid head-groups into the pore lining.     

Atomic scale structure and functional models of voltage-gated potassium channels.

Recent mutagenesis experiments have confirmed our hypothesis that a segment between S5 and S6 forms the ion selective portion of voltage-gated ion channels. Based on these and other new data, we have revised previous models of the general folding pattern of voltage-gated channel proteins and have developed atomic scale models of the entire transmembrane region of the Shaker A K+ channel. In these models, the ion selective region is a beta-barrel that spans the outer half of the membrane. The inner half of the pore is larger. The voltage-dependent conformational changes of activation gating are modeled to occur by the "helical screw" mechanism, in which the four S4 segments move along and rotate about their axes. These changes are followed by a voltage-independent conformational change, in which the segments linking S4 to S5 move from blocking the intracellular entrance of the pore to forming part of the lining of the large inner portion of the pore. The NH2-terminal of the protein was modeled as an alpha-helix that plugs the intracellular half of the pore to inactivate the channel.     

Glandularia X hybrida (Verbenaceae), a new combination for a common horticultural plant

A new combination,Glandularia x hybrida, and a lectotype are proposed for the common Garden Vervain (Verbena xhybrida). The plant is of horticultural origin, but occurs widely in North America and Mexico as an adventive.     

A new species of Ionactis (Asteraceae: Astereae) from Southern Nevada and an overview of the genus

Ionactis caelestis Leary & Nesom is a new species known from a single population that occurs on the Aztec Sandstone near Bridge Mountain in the Spring Mountains of Clark County, Nevada. It is placed in the genus Ionactis (=Aster subg. Ianthe) on the basis of its crowded, multicipital crown, lack of persistent basal leaves and presence of densely arranged cauline ones, strongly carinate phyllaries, blue rays, disc style branches with linear-lanceolate appendages, asymmetric carpopodia, double pappus, and chromosome number of 2n = 9 II. A key to the four species of the genus emphasizes the distinction of the new species in its taproot, the abundant, large, glandular trichomes on its stems and leaves, and disc flowers with sterile ovaries. Ionactis is more similar to the goldenaster (Heterotheca) lineage than to Aster, with which it has been allied formerly. The core of the goldenaster genera differ from Ionactis primarily in their yellow-rayed heads, the crystal complement within cells of their disc corollas, and their primarily multinerved achenes.     

A naphthyl analog of the aminostyryl pyridinium class of potentiometric membrane dyes shows consistent sensitivity in a variety of tissue,cell, and model membrane preparations

The fast potentiometric indicator di-4-ANEPPS is examined in four different preparations: lipid vesicles, red blood cells, squid giant axon, and guinea pig heart. The dye gives consistent potentiometric responses in each of these systems, although some of the detailed behavior varies. In lipid vesicles, the dye displays an increase in fluorescence combined with a red shift of the excitation spectrum upon hyperpolarization. Similar behavior is found in red cells where a dual wavelength radiometric measurement is also demonstrated. The signal-to-noise ratio of the potentiometric fluorescence response is among the best ever recorded on the voltage-clamped squid axon. The dye is shown to be a faithful and persistent monitor of cardiac action potentials with no appreciable loss of signal or deterioration of cardiac activity for periods as long as 2 hr with intermittent illumination every 10 min. These results, together with previously published applications of the dye to a spherical lipid bilayer model and to cells in culture, demonstrate the versatility of di-4-ANEPPS as a fast indicator of membrane potential.