Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:18217748rdf:typepubmed:Citationlld:pubmed
pubmed-article:18217748lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:18217748lifeskim:mentionsumls-concept:C0444498lld:lifeskim
pubmed-article:18217748pubmed:issue7lld:pubmed
pubmed-article:18217748pubmed:dateCreated2008-2-14lld:pubmed
pubmed-article:18217748pubmed:abstractTextWe have investigated the orientation and conformation of protein molecules at the polystyrene (PS)/protein solution interface using sum frequency generation (SFG) vibrational spectroscopy, supplemented by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). In this research, we studied fibrinogen as a model protein. SFG studies indicate that fibrinogen adopts a bent structure after adsorbing to the PS surface. A broad orientation distribution of fibrinogen coiled-coils at the interface has been quantified by combining SFG and ATR-FTIR measurements. Error analysis for such a deduced distribution was carried out. This research demonstrates that quantitative structural information such as orientational and conformational ordering of proteins at interfaces can be studied using SFG supplemented by other spectroscopic techniques.lld:pubmed
pubmed-article:18217748pubmed:languageenglld:pubmed
pubmed-article:18217748pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18217748pubmed:citationSubsetIMlld:pubmed
pubmed-article:18217748pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18217748pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18217748pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18217748pubmed:statusMEDLINElld:pubmed
pubmed-article:18217748pubmed:monthFeblld:pubmed
pubmed-article:18217748pubmed:issn1520-6106lld:pubmed
pubmed-article:18217748pubmed:authorpubmed-author:WangJieJlld:pubmed
pubmed-article:18217748pubmed:authorpubmed-author:LeeSang-HoSHlld:pubmed
pubmed-article:18217748pubmed:authorpubmed-author:ChenZhanZlld:pubmed
pubmed-article:18217748pubmed:issnTypePrintlld:pubmed
pubmed-article:18217748pubmed:day21lld:pubmed
pubmed-article:18217748pubmed:volume112lld:pubmed
pubmed-article:18217748pubmed:ownerNLMlld:pubmed
pubmed-article:18217748pubmed:authorsCompleteYlld:pubmed
pubmed-article:18217748pubmed:pagination2281-90lld:pubmed
pubmed-article:18217748pubmed:meshHeadingpubmed-meshheading:18217748...lld:pubmed
pubmed-article:18217748pubmed:meshHeadingpubmed-meshheading:18217748...lld:pubmed
pubmed-article:18217748pubmed:meshHeadingpubmed-meshheading:18217748...lld:pubmed
pubmed-article:18217748pubmed:meshHeadingpubmed-meshheading:18217748...lld:pubmed
pubmed-article:18217748pubmed:meshHeadingpubmed-meshheading:18217748...lld:pubmed
pubmed-article:18217748pubmed:meshHeadingpubmed-meshheading:18217748...lld:pubmed
pubmed-article:18217748pubmed:year2008lld:pubmed
pubmed-article:18217748pubmed:articleTitleQuantifying the ordering of adsorbed proteins in situ.lld:pubmed
pubmed-article:18217748pubmed:affiliationDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.lld:pubmed
pubmed-article:18217748pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18217748pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:18217748pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18217748lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18217748lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18217748lld:pubmed