pubmed-article:19879180 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19879180 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
pubmed-article:19879180 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:19879180 | lifeskim:mentions | umls-concept:C0376594 | lld:lifeskim |
pubmed-article:19879180 | pubmed:issue | 5-6 | lld:pubmed |
pubmed-article:19879180 | pubmed:dateCreated | 2009-12-2 | lld:pubmed |
pubmed-article:19879180 | pubmed:abstractText | Simple surfactants achieve remarkable long-range order in aqueous environments. This organizing potential is seen most dramatically in biological membranes where phospholipid assemblies both define cell boundaries and provide a ubiquitous structural scaffold for controlling cellular chemistry. Here we consider simple peptides that also spontaneously assemble into exceptionally ordered scaffolds, and review early data suggesting that these structures maintain the functional diversity of proteins. We argue that such scaffolds can achieve the required molecular order and catalytic agility for the emergence of chemical evolution. | lld:pubmed |
pubmed-article:19879180 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19879180 | pubmed:language | eng | lld:pubmed |
pubmed-article:19879180 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19879180 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19879180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19879180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19879180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19879180 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19879180 | pubmed:month | Dec | lld:pubmed |
pubmed-article:19879180 | pubmed:issn | 1879-0402 | lld:pubmed |
pubmed-article:19879180 | pubmed:author | pubmed-author:LynnDavid GDG | lld:pubmed |
pubmed-article:19879180 | pubmed:author | pubmed-author:MehtaAnil KAK | lld:pubmed |
pubmed-article:19879180 | pubmed:author | pubmed-author:RongNiN | lld:pubmed |
pubmed-article:19879180 | pubmed:author | pubmed-author:ChildersW... | lld:pubmed |
pubmed-article:19879180 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19879180 | pubmed:volume | 13 | lld:pubmed |
pubmed-article:19879180 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19879180 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19879180 | pubmed:pagination | 652-9 | lld:pubmed |
pubmed-article:19879180 | pubmed:dateRevised | 2011-3-3 | lld:pubmed |
pubmed-article:19879180 | pubmed:meshHeading | pubmed-meshheading:19879180... | lld:pubmed |
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pubmed-article:19879180 | pubmed:meshHeading | pubmed-meshheading:19879180... | lld:pubmed |
pubmed-article:19879180 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19879180 | pubmed:articleTitle | Peptide membranes in chemical evolution. | lld:pubmed |
pubmed-article:19879180 | pubmed:affiliation | Center for Fundamental and Applied Molecular Evolution and Center for Chemical Evolution, Department of Chemistry and Biology, Emory University, Atlanta, GA, United States. | lld:pubmed |
pubmed-article:19879180 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19879180 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:19879180 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:19879180 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19879180 | lld:pubmed |