CURRENT NOISE REVEALS PROTONATION KINETICS AND NUMBER OF IONIZABLE SITES IN AN OPEN PROTEIN ION CHANNEL
CURRENT NOISE REVEALS PROTONATION KINETICS AND NUMBER OF IONIZABLE SITES IN AN OPEN PROTEIN ION CHANNEL
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DOI：
10.1103/physrevlett.70.2352
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发表时间：
1993-04-12
影响因子：
8.6
通讯作者：
KASIANOWICZ, JJ
中科院分区：
文献类型：
--
作者：
BEZRUKOV, SM;KASIANOWICZ, JJ
类似于在固态电子微结构器件中发现的电流波动，观察到了由跨膜离子通道中位置的可逆电离产生的过量噪声。通过分析通过由α-毒素蛋白形成的完全开放的单通道的电流随pH的波动，我们能够评估质子化速率常数、参与质子化过程的位置数量以及单个位置重新充电对通道电导的影响。
In analogy to current fluctuations found in solid state electronic microstructure devices, excess noise generated by the reversible ionization of sites in a transmembrane ionic channel was observed. By analyzing the pH-dependent fluctuations in the current through fully open single channels formed by the alpha-toxin protein, we were able to evaluate the protonation rate constants, the number of sites participating in the protonation process, and the effect of recharging a single site on the channel conductance.