These days, many motorcycles have meager or nonexistent toolkits. On the road you may not be able to do extensive repairs, but you should be able to tighten a loose mirror and adjust your controls or suspension. CruzTOOLS makes specialized tools and toolkits for motorcyclists covering a wide range of applications, from specific brands such as Harley-Davidson and BMW to more universal kits. Two of our favorites are the DMX2 and RoadTech M3. Aimed at dual-sport/off-road riders, the 4.5-pound DMX2 packs essential tools into a durable, two-sided zippered pouch with an extra storage pocket (we added a siphon hose, tow strap and JB Weld), and it comes with a raincover and straps for mounting to an off-road-style front fender. The 3-pound RoadTech M3 is a compact, well-stocked tool roll for metric cruisers, sport tourers, etc. that we carry with us on road tests.Read our review of the CruzTOOLS RoadTech M3 metric motorcycle toolkit
Prism Essential Channel List
Potassium ion channels remove the hydration shell from the ion when it enters the selectivity filter. The selectivity filter is formed by a five residue sequence, TVGYG, termed the signature sequence, within each of the four subunits. This signature sequence is within a loop between the pore helix and TM2/6, historically termed the P-loop. This signature sequence is highly conserved, with the exception that a valine residue in prokaryotic potassium channels is often substituted with an isoleucine residue in eukaryotic channels. This sequence adopts a unique main chain structure, structurally analogous to a nest protein structural motif. The four sets of electronegative carbonyl oxygen atoms are aligned toward the center of the filter pore and form a square anti-prism similar to a water-solvating shell around each potassium binding site. The distance between the carbonyl oxygens and potassium ions in the binding sites of the selectivity filter is the same as between water oxygens in the first hydration shell and a potassium ion in water solution, providing an energetically-favorable route for de-solvation of the ions. Sodium ions, however, are too small to fill the space between the carbonyl oxygen atoms. Thus, it is energetically favorable for sodium ions to remain bound with water molecules in the extracellular space, rather than to pass through the potassium-selective ion pore.[61] This width appears to be maintained by hydrogen bonding and van der Waals forces within a sheet of aromatic amino acid residues surrounding the selectivity filter.[56][62] The selectivity filter opens towards the extracellular solution, exposing four carbonyl oxygens in a glycine residue (Gly79 in KcsA). The next residue toward the extracellular side of the protein is the negatively charged Asp80 (KcsA). This residue together with the five filter residues form the pore that connects the water-filled cavity in the center of the protein with the extracellular solution.[63] 2ff7e9595c
Comments