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Journal article

Subunit dimers of alpha-hemolysin expand the engineering toolbox for protein nanopores.

Abstract:

Staphylococcal α-hemolysin (αHL) forms a heptameric pore that features a 14-stranded transmembrane β-barrel. We attempted to force the αHL pore to adopt novel stoichiometries by oligomerizing subunit dimers generated by in vitro transcription and translation of a tandem gene. However, in vitro transcription and translation also produced truncated proteins, monomers, that were preferentially incorporated into oligomers. These oligomers were shown to be functional heptamers by single-channel re...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m111.218164

Authors


Journal:
The Journal of biological chemistry
Volume:
286
Issue:
16
Pages:
14324-14334
Publication date:
2011-04-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:6119cfc8-9af8-4f9d-9805-b428be3384e5
Source identifiers:
118072
Local pid:
pubs:118072

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