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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1994-7-8
|
| pubmed:abstractText |
Transmembrane alpha-helices can associate with one another in lipid bilayers. This association is important in the folding and oligomerization of many integral membrane proteins, and may also play a role in their function. The interactions between helices may be highly specific or relatively non-specific, and their roles may differ accordingly. These two cases are discussed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
6
|
| pubmed:volume |
346
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
17-20
|
| pubmed:dateRevised |
2005-11-16
|
| pubmed:meshHeading |
pubmed-meshheading:8206151-Amino Acid Sequence,
pubmed-meshheading:8206151-Lipid Bilayers,
pubmed-meshheading:8206151-Macromolecular Substances,
pubmed-meshheading:8206151-Membrane Proteins,
pubmed-meshheading:8206151-Models, Molecular,
pubmed-meshheading:8206151-Protein Folding,
pubmed-meshheading:8206151-Protein Structure, Secondary
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Specificity and promiscuity in membrane helix interactions.
|
| pubmed:affiliation |
Department of Pharmacology, New York University Medical Center, NY 10016.
|
| pubmed:publicationType |
Journal Article,
Review
|