Download PDF by Novartis Foundation: Ion Channels: From Atomic Resolution Physiology to

By Novartis Foundation

ISBN-10: 0470843756

ISBN-13: 9780470843758

ISBN-10: 0470868740

ISBN-13: 9780470868744

Ion channels offer a different chance to exploit computational methods to aim an realizing of the functionality of a membrane protein, beginning with an atomic answer constitution and progressing via a hierarchy of theoretical descriptions until eventually you'll be able to account quantitatively for his or her physiological functionality. This booklet brings jointly physiologists, structural biologists and theorists who got here jointly to assist outline the path of the sector within the rapid destiny. subject matters coated comprise: * the x-ray constitution of channels and pores * desktop simulation of channel functionality * specific information on potassium channels, chloride and calcium channels, and ligand-gated ion channels

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Read Online or Download Ion Channels: From Atomic Resolution Physiology to Functional Genomics -No. 245 (Novartis Foundation Symposia) PDF

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Additional info for Ion Channels: From Atomic Resolution Physiology to Functional Genomics -No. 245 (Novartis Foundation Symposia)

Sample text

Locations of the NPA motifs, an observation that disagrees with results reported by Murata et al (2000). This narrow pore, which acts as the size-selective filter to exclude small solutes, bends by ~25° as it traverses the bilayer (Fig. 4B). The apex of the curvilinear pathway is close to the middle of the bilayer where the inplane pseudo twofold axis of symmetry is also located. Thus, the ~ 18 A long, narrow part of the channel includes a region of the molecule where the approximate twofold symmetry is the strongest (Cheng et al 1997, Ren et al 2000a), leading to a symmetrical environment that is consistent with observed bidirectional water flow (Meinild et al 1998).

But not a lot. On the other hand, in this 20+10+5-fold averaged structure, we can follow the run of the main chain pretty well. There is not a lot of disorder in this structure. C3n the other hand, if 20-30% of the molecules were disordered, I am not sure you would lose that density entirely. It is hard to tell. Miller: I don't recollect that anyone has reported that HEPES activates ACh receptors. The known structure-activity relationships would make it unlikely to be an agonist or competitive antagonist.

Note the location of the 'tyrosine cornerstone'. This residue is not present in AChBP, but is replaced by the conserved disulfide bridge. complementary parts of the binding pocket, respectively (Corringer et al 2000). The a-subunit residues important for binding are clustered in 'loop' regions, A (Galzi et al 1990), B (Dennis et al 1988) and C (Dennis et al 1988, Kao et al 1984, Sine et al 1994). The a subunit contributes the primary binding site, consisting of loop A, B and C. The neighbouring subunit, g or d, contributes 'loops' D (Chiara & Cohen 1997), E (Chiara & Cohen 1997, Chiara et al 1999, Sine 1997) and F (Czajkowski & Karlin 1995) (Table 1); in homopentamers the equivalent loops will be contributed by a subunits.

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Ion Channels: From Atomic Resolution Physiology to Functional Genomics -No. 245 (Novartis Foundation Symposia) by Novartis Foundation


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