| pubmed-article:15755453 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C0003320 | lld:lifeskim |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C0808080 | lld:lifeskim |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C1705922 | lld:lifeskim |
| pubmed-article:15755453 | lifeskim:mentions | umls-concept:C0872367 | lld:lifeskim |
| pubmed-article:15755453 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15755453 | pubmed:dateCreated | 2005-3-9 | lld:pubmed |
| pubmed-article:15755453 | pubmed:abstractText | We investigated molecular recognition of antibodies to membrane-antigens and extraction of the antigens out of membranes at the single molecule level. Using dynamic force microscopy imaging and enzyme immunoassay, binding of anti-sendai antibodies to sendai-epitopes genetically fused into bacteriorhodopsin molecules from purple membranes were detected under physiological conditions. The antibody/antigen interaction strength of 70-170 pN at loading rates of 2-50 nN/second yielded a barrier width of x = 0.12 nm and a kinetic off-rate (corresponding to the barrier height) of k(off) = 6s(-1), respectively. Bacteriorhodopsin unfolding revealed a characteristic intra-molecular force pattern, in which wild-type and sendai-bacteriorhodopsin molecules were clearly distinguishable in their length distributions, originating from the additional 13 amino acid residues epitope in sendai purple membranes. The inter-molecular antibody/antigen unbinding force was significantly lower than the force required to mechanically extract the binding epitope-containing helix pair out of the membrane and unfold it (126 pN compared to 204 pN at the same loading rate), meeting the expectation that inter-molecular unbinding forces are weaker than intra-molecular unfolding forces responsible for stabilizing native conformations of proteins. | lld:pubmed |
| pubmed-article:15755453 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15755453 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15755453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15755453 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15755453 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15755453 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:15755453 | pubmed:author | pubmed-author:HinterdorferP... | lld:pubmed |
| pubmed-article:15755453 | pubmed:author | pubmed-author:KadaGeraldG | lld:pubmed |
| pubmed-article:15755453 | pubmed:author | pubmed-author:KienbergerFer... | lld:pubmed |
| pubmed-article:15755453 | pubmed:author | pubmed-author:MuellerHarald... | lld:pubmed |
| pubmed-article:15755453 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15755453 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15755453 | pubmed:volume | 347 | lld:pubmed |
| pubmed-article:15755453 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15755453 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15755453 | pubmed:pagination | 597-606 | lld:pubmed |
| pubmed-article:15755453 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
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| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
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| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:meshHeading | pubmed-meshheading:15755453... | lld:pubmed |
| pubmed-article:15755453 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15755453 | pubmed:articleTitle | Single molecule studies of antibody-antigen interaction strength versus intra-molecular antigen stability. | lld:pubmed |
| pubmed-article:15755453 | pubmed:affiliation | Institute for Biophysics, University of Linz, Altenbergerstr. 69, A-4040 Linz, Austria. | lld:pubmed |
| pubmed-article:15755453 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15755453 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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