Ontology highlight
ABSTRACT:
SUBMITTER: Maglia G
PROVIDER: S-EPMC2604925 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
Maglia Giovanni G Restrepo Marcela Rincon MR Mikhailova Ellina E Bayley Hagan H
Proceedings of the National Academy of Sciences of the United States of America 20081205 50
Both protein and solid-state nanopores are under intense investigation for the analysis of nucleic acids. A crucial advantage of protein nanopores is that site-directed mutagenesis permits precise tuning of their properties. Here, by augmenting the internal positive charge within the alpha-hemolysin pore and varying its distribution, we increase the frequency of translocation of a 92-nt single-stranded DNA through the pore at +120 mV by approximately 10-fold over the wild-type protein and dramat ...[more]