Shin-Ho Chung, Olaf S. Anderson, Vikram V. Krishnamurthy's Biological Membrane Ion Channels. Dynamics, Structure and PDF

By Shin-Ho Chung, Olaf S. Anderson, Vikram V. Krishnamurthy

ISBN-10: 0387333231

ISBN-13: 9780387333236

Ion channels are organic nanotubes which are shaped via membrane proteins. simply because ion channels keep an eye on all electric actions in residing cells, figuring out their mechanisms at a molecular point is a basic challenge in biology. This booklet offers with fresh breakthroughs in ion-channel learn which were caused through the mixed attempt of experimental biophysicists and computational physicists, who jointly are starting to resolve the tale of those exquisitely designed biomolecules. With chapters via best specialists, the booklet is aimed toward researchers in nanodevices and biosensors, in addition to complicated undergraduate and graduate scholars in biology and the actual sciences.
Key Features
- provides the newest info at the molecular mechanisms of ion permeation via membrane ion channels
- makes use of schematic diagrams to demonstrate vital recommendations in biophysics
- encompasses a CD-ROM with laptop courses used for making theoretical calculations, in addition to video animations illustrating numerous positive aspects of ion channels
- Written by way of best researchers within the quarter of ion channel investigations

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Extra resources for Biological Membrane Ion Channels. Dynamics, Structure and Applns

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Huxley. 1952a. Currents carried by sodium and potassium ions through the membrane of the giant axon of Loligo. J. Physiol. 116:449–472. F. Huxley. 1952b. A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117:500–544. F. Huxley, and B. Katz. 1952. Measurement of current–voltage relations in the membrane of the giant axon of Loligo. J. Physiol. 116:424–448. D. Keynes. 1955. The potassium permeability of a giant nerve fibre. J. Physiol.

H. Takahashi, T. Tanabe, M. Toyosato, Y. Furutani, T. Hirose, M. Asai, S. Inayama, T. Miyata, and S. Numa. 1982. Primary structure of alpha-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence. Nature 299:793–797. , H. Takahashi, T. Tanabe, M. Toyosato, S. Kikyotani, Y. Furutani, T. Hirose, H. Takashima, S. Inayama, T. Miyata, and S. Numa. 1983. Structural homology of Torpedo californica acetylcholine receptor subunits. Nature 302:528–532. 26 1. , L. Catacuzzeno, and B.

37 Olaf S. Andersen et al. 3 residues per turn are possible. 3 residues per helical turn (Urry, 1972). 3 helical dimers. More details concerning the early structural and functional evidence for this structure are summarized in Andersen and Koeppe (1992) and Andersen et al. (1999). , 1999), but see also Durkin et al. (1992) and Andersen et al. (1996). This structural resilience makes gA channels valuable as prototypical channels. , 2001). Though the solution NMR studies were done on gA incorporated into sodium dodecylsulfate micelles (SDS) and the solid-state NMR experiments were done on gA incorporated into oriented dimyristoylphosphatidylcholine (DMPC) bilayers, the results have converged to agreement upon one channel structure (Fig.

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Biological Membrane Ion Channels. Dynamics, Structure and Applns by Shin-Ho Chung, Olaf S. Anderson, Vikram V. Krishnamurthy


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