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. 2004 Dec 23;102(1):87–92. doi: 10.1073/pnas.0406777102

Table 1. Gating rate constants for AChR mutants.

Construct Predicted opening rate constant, β2 Predicted closing rate constant, α2
Slow-closing
δS268G 43,772 1,897
δS268C 78,566 363
δS268T 93,580 369
δS268V 107,468 131
δS268N 138,751 107
δL265′T 44,349 88
δL265′T+αD97C 191,457 91
δL265′T+αD97E 884,093 86
δL265′T+αD97Q 2.163E6 85
δL265′T+αD97A 4.972E6 72
Fast-opening
αD97N 96,630 1,617
αD97C 191,457 1,476
αD97M 301,068 1,532
αD97Y 503,342 1,354
αD97H 663,430 1,317
αD97E 883,372 1,410
αD97F 990,819 1,244
αD97Q 2,165E6 1,370
αD97R 3.948E6 1,123
αD97A 4.972E6 1,168

All values are s-1 and pertain to diliganded AChRs activated by ACh. The predicted opening and closing rate constants are calculated from the corresponding values measured for choline and using Eq 1 (see Materials and Methods). The calculated opening and closing rate constants for WT AChRs activated by ACh are 44,349 s-1 and 1,583 s-1, respectively, and are similar to the experimentally determined values of ≈48,000 s-1 and ≈1,700 s-1, respectively. The double-mutant constructs in the slow-closing series also open rapidly, but it is mainly their slow α-values that cause k* to approach zero and, hence, drive τb towards σ-1 (Eq. 3).