Electrical characterization of protein molecules by a solid-state nanopore
Electrical characterization of protein molecules by a solid-state nanopore
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DOI:
10.1063/1.2767206
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发表时间:
2007-07-30
影响因子:
4
通讯作者:
Li, Jiali
中科院分区:
文献类型:
--
作者:
Fologea, Daniel;Ledden, Bradley;Li, Jiali
The authors measured ionic current blockages caused by protein translocation through voltage-biased silicon nitride nanopores in ionic solution. By calculating the mean amplitude, time duration, and the integral of current blockages, they estimated the relative charge and size of protein molecules at a single molecule level. The authors measured the change in protein charge of bovine serum albumin (BSA) protein induced by pH variation. They also confirmed that BSA molecules indeed traverse nanopores using an improved chemiluminescent analysis. They demonstrated that a larger protein fibrinogen could be distinguished from BSA by a solid-state nanopore measurement. (C) 2007 American Institute of Physics.