Switch to
Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1996-10-18
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pubmed:abstractText |
Several porins from bacterial outer membranes have been crystallized and analyzed by X-ray diffraction, yielding a consistent picture of these membrane-channel proteins. The structures of general and specific channels are in agreement with electrophysiological, diffusional and biochemical data, and provide a starting point for the engineering of other passive membrane pores or porins with new selectivities.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
0959-440X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
485-90
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:8794162-Diffusion,
pubmed-meshheading:8794162-Drug Design,
pubmed-meshheading:8794162-Ion Channels,
pubmed-meshheading:8794162-Membrane Proteins,
pubmed-meshheading:8794162-Porins,
pubmed-meshheading:8794162-Protein Folding,
pubmed-meshheading:8794162-Protein Structure, Secondary,
pubmed-meshheading:8794162-Voltage-Dependent Anion Channels
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pubmed:year |
1996
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pubmed:articleTitle |
Porins: general to specific, native to engineered passive pores.
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pubmed:affiliation |
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Univer?ität, Albertstrasse 21, D-79104, Freiburg im Breisgau, Germany. schulz@bio5.chemie.uni-freiburg.de
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pubmed:publicationType |
Journal Article,
Review
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