| pubmed-article:18550546 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C0018165 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C2698172 | lld:lifeskim |
| pubmed-article:18550546 | lifeskim:mentions | umls-concept:C1708533 | lld:lifeskim |
| pubmed-article:18550546 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:18550546 | pubmed:dateCreated | 2008-8-4 | lld:pubmed |
| pubmed-article:18550546 | pubmed:abstractText | To better understand the structural and functional roles of tryptophan at the membrane/water interface in membrane proteins, we examined the structural and functional consequences of Trp --> 1-methyl-tryptophan substitutions in membrane-spanning gramicidin A channels. Gramicidin A channels are miniproteins that are anchored to the interface by four Trps near the C terminus of each subunit in a membrane-spanning dimer. We masked the hydrogen bonding ability of individual or multiple Trps by 1-methylation of the indole ring and examined the structural and functional changes using circular dichroism spectroscopy, size exclusion chromatography, solid state (2)H NMR spectroscopy, and single channel analysis. N-Methylation causes distinct changes in the subunit conformational preference, channel-forming propensity, single channel conductance and lifetime, and average indole ring orientations within the membrane-spanning channels. The extent of the local ring dynamic wobble does not increase, and may decrease slightly, when the indole NH is replaced by the non-hydrogen-bonding and more bulky and hydrophobic N-CH(3) group. The changes in conformational preference, which are associated with a shift in the distribution of the aromatic residues across the bilayer, are similar to those observed previously with Trp --> Phe substitutions. We conclude that indole N-H hydrogen bonding is of major importance for the folding of gramicidin channels. The changes in ion permeability, however, are quite different for Trp --> Phe and Trp --> 1-methyl-tryptophan substitutions, indicating that the indole dipole moment and perhaps also ring size and are important for ion permeation through these channels. | lld:pubmed |
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| pubmed-article:18550546 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18550546 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18550546 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18550546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18550546 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18550546 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18550546 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18550546 | pubmed:author | pubmed-author:AndersenOlaf... | lld:pubmed |
| pubmed-article:18550546 | pubmed:author | pubmed-author:GreathouseDen... | lld:pubmed |
| pubmed-article:18550546 | pubmed:author | pubmed-author:KoeppeRoger... | lld:pubmed |
| pubmed-article:18550546 | pubmed:author | pubmed-author:SunHaiyanH | lld:pubmed |
| pubmed-article:18550546 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18550546 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:18550546 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18550546 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18550546 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18550546 | pubmed:pagination | 22233-43 | lld:pubmed |
| pubmed-article:18550546 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18550546 | pubmed:meshHeading | pubmed-meshheading:18550546... | lld:pubmed |
