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A protein pore with a single polymer chain tethered within the lumen

Abstract:

A transmembrane protein pore with a single 5000 Da poly(ethylene glycol) (PEG) molecule attached covalently within the channel lumen has been constructed from seven staphylococcal α-hemolysin subunits. The modified heptamer is stable and can be purified by electrophoresis in sodium dodecyl sulfate, without dissociation of the subunits. The properties of the modified pore were studied by single channel current recording. The PEG molecule reduces the mean conductance of the pore by 18%, as woul...

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Publication status:
Published

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Publisher copy:
10.1021/ja993221h

Authors


Howorka, S More by this author
Movileanu, L More by this author
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Journal:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume:
122
Issue:
11
Pages:
2411-2416
Publication date:
2000-03-22
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:723f2261-ec50-4311-8b3c-54b1b245b002
Source identifiers:
278527
Local pid:
pubs:278527
Language:
English

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