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Biological Membrane Ion Channels: Dynamics, Structure, and by Peter C. Jordan (auth.), Shin-Ho Chung, Olaf S. Andersen, PDF

By Peter C. Jordan (auth.), Shin-Ho Chung, Olaf S. Andersen, Vikram Krishnamurthy (eds.)

ISBN-10: 0387333231

ISBN-13: 9780387333236

ISBN-10: 0387689192

ISBN-13: 9780387689197

Ion channels are organic nanotubes which are shaped by way of membrane proteins. simply because ion channels control all electric actions in dwelling cells, realizing their mechanisms at a molecular point is a primary challenge in biology. This publication offers with contemporary breakthroughs in ion-channel examine which were led to by means of the mixed attempt of experimental biophysicists and computational physicists, who jointly are commencing to get to the bottom of the tale of those exquisitely designed biomolecules. With chapters by way of top specialists, the ebook is geared toward researchers in nanodevices and biosensors, in addition to complicated undergraduate and graduate scholars in biology and the actual sciences.
Key Features
Presents the most recent details at the molecular mechanisms of ion permeation via membrane ion channels
Uses schematic diagrams to demonstrate vital suggestions in biophysics
Written by means of major researchers within the zone of ion channel investigations

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Additional info for Biological Membrane Ion Channels: Dynamics, Structure, and Applications

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J. Membr. Biol. 30:99–120. , K. A. J. Sigworth. 1992. The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255:1712–1715. , and A. Warshel. 2001. What are the dielectric “constants” of proteins and how to validate electrostatic models? Proteins 44:400–417. , and P. Agre. 1991. Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266:6407– 6415. G. K. Lee, P. K. Jap. 2001. Structural basis of waterspecific transport through the AQP1 water channel.

Miller, F. R. Selvin. 2005. Small vertical movement of a KC channel voltage sensor measured with luminescence energy transfer. Nature 436:848–851. , U. Ludewig, A. J. Jentsch. 1995. Gating of the voltagedependent chloride channel CLC-0 by the permeant anion. Nature 373:527– 531. W. D. E. Hood. 1980. Acetylcholine receptor: Complex of homologous subunits. Science 208:1454–1456. , M. Milescu, Y. A. I. J. Swartz. 2005. Voltage-sensor activation with a tarantula toxin as cargo. 436:857–860. , C. Methfessel, M.

6 residues per helical turn, crystallized from ethanol, PDB:1ALZ (Langs, 1988). 3 -helical structure in Fig. 3, the two subunits are shaded differently, and the formyl oxygens and indole NH’s are black. In contrast to Fig. 3, the Trp indole rings in the DS structures do not cluster near the ends (the membrane/solution interfaces), but are distributed quite evenly along the dimer. the Trp indole rings (cf. Figs. 5). When the DS conformers encounter lipid bilayer membranes, they unfold/refold into the Trp-anchored SS structure in Fig.

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Biological Membrane Ion Channels: Dynamics, Structure, and Applications by Peter C. Jordan (auth.), Shin-Ho Chung, Olaf S. Andersen, Vikram Krishnamurthy (eds.)


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