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edited by F. C. NEIDHARDT (ASM, Washington)
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STOCK J. and SURETTE M., in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, edited by F. C. NEIDHARDT (ASM, Washington) 1996; FALKE J. J. et al., Annu. Rev. Cell Dev. Biol., 13 (1997) 457; BLAIR D. F., Annu. Rev. Microbiol., 49 (1995) 489.
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Stock, J.1
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Falke, J.J.1
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0028822933
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Blair, D.F.1
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Segall, J.E.1
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Khan, S.4
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10
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0002246461
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note
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2 are exactly zero, i.e. the adaptation is perfect. The viewpoint of evolution may thus help us to understand why the adaptation has to be perfect. On the other hand, an underlying physical mechanism needs to be found.
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11
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0033552946
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ALON U., SURETTE M. G., BARKAI N. and LEIBLER S., Nature, 397 (1999) 168.
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Alon, U.1
Surette, M.G.2
Barkai, N.3
Leibler, S.4
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13
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0002113977
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note
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The time scale of ligand debinding ranges from tens of seconds to tens of minutes, longer than the signalling time scale, i.e. the time scale for achieving the temporally local equilibrium, as discussed below. This quenched disorder model is thus more favorable than a grand-canonical ensemble approach, which would treat binding-debinding processes as a part of the process towards equilibrium. Although we are not sure whether the debinding time scale is always longer than the time to complete the adaptation, this does not matter, because on the coarse-grained time scale, eq. (6) is always valid, independent of which of the receptors are liganded.
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14
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0002107507
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note
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0 is the solution to 0 = 2c/1 + exp[ - 2β (νJcursive Greek chi + B)] + 2(1-c)/1 + exp[ - 2βνJcursive Greek chi] - 1. To understand this, consider m(τ - 1) as the cursive Greek chi coordinate of the cross between y = cursive Greek chi and y = f(cursive Greek chi), while m(τ) as the cursive Greek chi coordinate of the cross between y = cursive Greek chi and y = f[cursive Greek chi - σ/νJm(τ - 1)], which is obtained by translating y = f(cursive Greek chi) along the cursive Greek chi-direction.
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17
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0002179307
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note
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We conjecture that which subunit provides the mobile helix may be random, and that dimerization of receptors might provide a redundancy so that if one subunit is damaged, the other can work as an alternative. The negative cooperativity between the two subunits may be due to an "antiforromagnetic" coupling.
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