| pubmed-article:17443187 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17443187 | lifeskim:mentions | umls-concept:C0034792 | lld:lifeskim |
| pubmed-article:17443187 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:17443187 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:17443187 | pubmed:issue | 7138 | lld:pubmed |
| pubmed-article:17443187 | pubmed:dateCreated | 2007-4-19 | lld:pubmed |
| pubmed-article:17443187 | pubmed:abstractText | Muscle contraction is triggered by the opening of acetylcholine receptors at the vertebrate nerve-muscle synapse. The M2 helix of this allosteric membrane protein lines the channel, and contains a 'gate' that regulates the flow of ions through the pore. We used single-molecule kinetic analysis to probe the transition state of the gating conformational change and estimate the relative timing of M2 motions in the alpha-subunit of the murine acetylcholine receptor. This analysis produces a 'Phi-value' for a given residue that reflects its open-like versus closed-like character at the transition state. Here we show that most of the residues throughout the length of M2 have a Phi-value of approximately 0.64 but that some near the middle have lower Phi-values of 0.52 or 0.31, suggesting that alphaM2 moves in three discrete steps. The core of the channel serves both as a gate that regulates ion flow and as a hub that directs the propagation of the gating isomerization through the membrane domain of the acetylcholine receptor. | lld:pubmed |
| pubmed-article:17443187 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17443187 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17443187 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17443187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17443187 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17443187 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17443187 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17443187 | pubmed:issn | 1476-4687 | lld:pubmed |
| pubmed-article:17443187 | pubmed:author | pubmed-author:AuerbachAntho... | lld:pubmed |
| pubmed-article:17443187 | pubmed:author | pubmed-author:MitraAnanyaA | lld:pubmed |
| pubmed-article:17443187 | pubmed:author | pubmed-author:PurohitPrasad... | lld:pubmed |
| pubmed-article:17443187 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17443187 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:17443187 | pubmed:volume | 446 | lld:pubmed |
| pubmed-article:17443187 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17443187 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17443187 | pubmed:pagination | 930-3 | lld:pubmed |
| pubmed-article:17443187 | pubmed:meshHeading | pubmed-meshheading:17443187... | lld:pubmed |
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| pubmed-article:17443187 | pubmed:meshHeading | pubmed-meshheading:17443187... | lld:pubmed |
| pubmed-article:17443187 | pubmed:meshHeading | pubmed-meshheading:17443187... | lld:pubmed |
| pubmed-article:17443187 | pubmed:meshHeading | pubmed-meshheading:17443187... | lld:pubmed |
| pubmed-article:17443187 | pubmed:meshHeading | pubmed-meshheading:17443187... | lld:pubmed |
| pubmed-article:17443187 | pubmed:meshHeading | pubmed-meshheading:17443187... | lld:pubmed |
| pubmed-article:17443187 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17443187 | pubmed:articleTitle | A stepwise mechanism for acetylcholine receptor channel gating. | lld:pubmed |
| pubmed-article:17443187 | pubmed:affiliation | Department of Physiology and Biophysics, State University of New York at Buffalo, Buffalo, New York 14214, USA. | lld:pubmed |
| pubmed-article:17443187 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17443187 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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