pubmed-article:9521110 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C0023768 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C0587267 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9521110 | lifeskim:mentions | umls-concept:C0009284 | lld:lifeskim |
pubmed-article:9521110 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9521110 | pubmed:dateCreated | 1998-5-21 | lld:pubmed |
pubmed-article:9521110 | pubmed:abstractText | The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190 residue C-terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid-state NMR spectroscopy in oriented membrane bilayers. The 15N-NMR spectra of the colicin E1 show that: (1) the structure and dynamics are independent of anionic lipid content in both oriented and unoriented samples; (2) assuming the secondary structure of the polypeptide is helical, there are both trans-membrane and in-plane helical segments; (3) trans-membrane helices account for approximately 20-25% of the channel polypeptide, which is equivalent to 38-48 residues of the 190-residue polypeptide. The results of the two-dimensional PISEMA spectrum are interpreted in terms of a single trans-membrane helical hairpin inserted into the bilayer from each channel molecule. These data are also consistent with this helical hairpin being derived from the 38-residue hydrophobic segment near the C-terminus of the colicin E1 channel polypeptide. | lld:pubmed |
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pubmed-article:9521110 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9521110 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9521110 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9521110 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9521110 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:9521110 | pubmed:author | pubmed-author:CramerW AWA | lld:pubmed |
pubmed-article:9521110 | pubmed:author | pubmed-author:OpellaS JSJ | lld:pubmed |
pubmed-article:9521110 | pubmed:author | pubmed-author:KimYY | lld:pubmed |
pubmed-article:9521110 | pubmed:author | pubmed-author:ValentiniGG | lld:pubmed |
pubmed-article:9521110 | pubmed:author | pubmed-author:SchendelS LSL | lld:pubmed |
pubmed-article:9521110 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9521110 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:9521110 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9521110 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9521110 | pubmed:pagination | 342-8 | lld:pubmed |
pubmed-article:9521110 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:9521110 | pubmed:meshHeading | pubmed-meshheading:9521110-... | lld:pubmed |
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pubmed-article:9521110 | pubmed:meshHeading | pubmed-meshheading:9521110-... | lld:pubmed |
pubmed-article:9521110 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9521110 | pubmed:articleTitle | Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers. | lld:pubmed |
pubmed-article:9521110 | pubmed:affiliation | Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA. | lld:pubmed |
pubmed-article:9521110 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9521110 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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