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rdf:type |
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lifeskim:mentions |
umls-concept:C0009284,
umls-concept:C0023768,
umls-concept:C0024485,
umls-concept:C0439799,
umls-concept:C0587267,
umls-concept:C1442792,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2603343
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pubmed:issue |
2
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pubmed:dateCreated |
1998-5-21
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1284805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1373773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1445847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1510921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1702993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1710937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1726781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1765084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-18466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-1925542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-2611210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-3306759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-4960161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-6304732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-6309789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-7037787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-7507175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-7521016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-7545041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-7683055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8090709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8119982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8256289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8268153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8382373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8411155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8520224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8611578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-8744315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-9050156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9521110-9238014
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
342-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1998
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pubmed:articleTitle |
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
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pubmed:affiliation |
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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