- Abstract:
-
Extended retro (reversed) peptide sequences have not previously been accommodated within functional proteins. Here, we show that the entire transmembrane portion of the beta-barrel of the pore-forming protein alpha-hemolysin can be formed by retrosequences comprising a total of 175 amino acid residues, 25 contributed by the central sequence of each subunit of the heptameric pore. The properties of wild-type and retro heptamers in planar bilayers are similar. The single-channel conductance of ...
Expand abstract - Publication status:
- Published
- Publisher:
- Cambridge University Press
- Journal:
- Protein science : a publication of the Protein Society
- Volume:
- 8
- Issue:
- 6
- Pages:
- 1257-1267
- Publication date:
- 1999-06-05
- DOI:
- EISSN:
-
1469-896X
- ISSN:
-
0961-8368
- URN:
-
uuid:95ab9545-b474-4487-ab89-1dc0bfe1bdc5
- Source identifiers:
-
52186
- Local pid:
- pubs:52186
- Copyright date:
- 1999
Journal article
A functional protein pore with a "retro" transmembrane domain.
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