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Proteins conductivity

Photosensitivie proteins (conducting polymer) Photosynthetic reaction... [Pg.200]

Spahn CM, Beckmann R, Eswar N, Penczek PA, Sali A, Blobel G, Frank J, Helmers J (2001) Structure of the 80S ribosome from Saccharomyces cerevisiae—tRNA-ribosome and subunit-subunit interactions architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 107 373-386... [Pg.28]

Tim23 forms a protein-conducting channel that is regulated by the action of Tim50, and Timl7 (Martinez-Caballero et al. 2006 Meinecke et al. [Pg.27]

Mitra et al. (2005) Structure of the E. coli protein-conducting channel bound to a translating ribosome. Nature 438 318-324... [Pg.69]

Beckmann, R., Spahn, C. M. T., Eswar, N., Helmers, J., Penczek, P. A., Sali, A., Frank, J., and Blobel, G. (2001). Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 107, 361-372. [Pg.14]

Simon, S-, and BlobeJ, G. (1991). A protein-conducting channel in the endoplasmic reticulum, Cell 6S, 37l-m... [Pg.56]

The Translocon. The SRP SR complex delivers the ribosome to the ER membrane. There it docks with the translocation machinery, called the translocon, a multisubunit assembly of integral and peripheral membrane proteins. The translocon is a protein-conducting channel. This channel opens when the translocon and ribosome bind to each other. Protein synthesis resumes with the growing polypeptide chain passing through the translocon channel into the lumen of the ER. [Pg.881]

Polypeptide chains are transported across the membrane through an aqueous channel formed from membrane proteins. This protein-conducting channel is transiently formed so that a polypeptide chain can move across the pho-spholipid bilayer. The protein-conducting channel exists for both co- and post-translational processes and opens in two dimensions, i.e. perpendicular to the membrane to let hydrophilic polypeptide chains cross, and within the plane of the membrane to let hydrophobic anchors of membrane proteins into the phospholipid bilayer. [Pg.489]

Maruccio G, Matzo P, Krahne R, Passaseo A, Cingolani R, Rinaldi R (2007) Protein conduction and negative differential resistance in large-scale nanojunction arrays. Small 3 1184—1188... [Pg.1866]

The most familiar type of electrokinetic experiment consists of setting up a potential gradient in a solution containing charged particles and determining their rate of motion. If the particles are small molecular ions, the phenomenon is called ionic conductance, if they are larger units, such as protein molecules, or colloidal particles, it is called electrophoresis. [Pg.183]

Other biomoleciiles imaged have included all DNA bases [44], polysaccharides [45] and proteins [46, 4lZ]. In many cases there is strong evidence that the imaging process is facilitated by the presence of iiltrathin (conducting) water films on the surface of the sample [48, 49 and 50],... [Pg.1685]

Mineralocorticoids foUow a mechanistic route similar to that of glucocorticoids, though differing in the proteins expressed. The activated MR-DNA complex promotes the expression of aldosterone-induced proteins (AIPs), which then act to increase conductance of the luminal membrane and concurrently increase pump activity of the basolateral membrane. These actions result from a number of AlP-influenced cellular characteristics,... [Pg.98]

Mode of Motion. Nicotine, anabasine, and imidocloprid affect the ganglia of the insect central nervous system, faciUtating transsynaptic conduction at low concentrations and blocking conduction at higher levels. The extent of ionisation of the nicotinoids plays an important role in both their penetration through the ionic barrier of the nerve sheath to the site of action and in their interaction with the site of action, which is befleved to be the acetylcholine receptor protein. There is a marked similarity in dimensions between acetylcholine and the nicotinium ion. [Pg.269]

Traditional appHcations for latices are adhesives, binders for fibers and particulate matter, protective and decorative coatings (qv), dipped goods, foam, paper coatings, backings for carpet and upholstery, modifiers for bitumens and concrete, and thread and textile modifiers. More recent appHcations include biomedical appHcations as protein immobilizers, visual detectors in immunoassays (qv), as release agents, in electronic appHcations as photoresists for circuit boards, in batteries (qv), conductive paint, copy machines, and as key components in molecular electronic devices. [Pg.23]

Calcium-binding protein is not found in the intestinal mucosa of vitamin D-deficient animals. It is synthesized only in response to the presence of a material with vitamin D activity. Thus, using antisemm specific to intestinal calcium-binding protein, a radioimmunodiffusion assay (98) conducted on ... [Pg.133]

After po dosing, verapamil s absorption is rapid and almost complete (>90%). There is extensive first-pass hepatic metabolism and only 10—35% of the po dose is bioavahable. About 90% of the dmg is bound to plasma proteins. Peak plasma concentrations are achieved in 1—2 h, although effects on AV nodal conduction may be apparent in 30 min (1—2 min after iv adrninistration). Therapeutic plasma concentrations are 0.125—0.400 p.g/mL. Verapamil is metabolized in the liver and 12 metabolites have been identified. The principal metabolite, norverapamil, has about 20% of the antiarrhythmic activity of verapamil (3). The plasma half-life after iv infusion is 2—5 h whereas after repeated po doses it is 4.5—12 h. In patients with liver disease the elimination half-life may be increased to 13 h. Approximately 50% of a po dose is excreted as metabolites in the urine in 24 h and 70% within five days. About 16% is excreted in the feces and about 3—4% is excreted as unchanged dmg (1,2). [Pg.121]


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