20815000

Source:http://linkedlifedata.com/resource/pubmed/id/20815000

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0162847, umls-concept:C0182400, umls-concept:C0332324, umls-concept:C0376534, umls-concept:C1510464, umls-concept:C1690862
pubmed:issue	41
pubmed:dateCreated	2010-11-1
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/1 S10 RR025072-1, http://linkedlifedata.com/resource/pubmed/grant/GM053640, http://linkedlifedata.com/resource/pubmed/grant/R01 GM053640-15, http://linkedlifedata.com/resource/pubmed/grant/R01 GM053640-16, http://linkedlifedata.com/resource/pubmed/grant/R01 GM053640-17
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0370543
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Alanine, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/azidohomoalanine, http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L9
pubmed:status	MEDLINE
pubmed:month	Oct
pubmed:issn	1521-3773
pubmed:author	pubmed-author:BanerjeePartha SPS, pubmed-author:CarricoIsaacI, pubmed-author:ChungJuahJ, pubmed-author:DyerR BrianRB, pubmed-author:NagarajanSureshbabuS, pubmed-author:RaleighDaniel PDP, pubmed-author:Taskent-SezginHumeyraH
pubmed:issnType	Electronic
pubmed:day	4
pubmed:volume	49
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	7473-5
pubmed:dateRevised	2011-11-10
pubmed:meshHeading	pubmed-meshheading:20815000-Alanine, pubmed-meshheading:20815000-Models, Molecular, pubmed-meshheading:20815000-Protein Conformation, pubmed-meshheading:20815000-Protein Folding, pubmed-meshheading:20815000-Protein Structure, Tertiary, pubmed-meshheading:20815000-Proteins, pubmed-meshheading:20815000-Ribosomal Proteins, pubmed-meshheading:20815000-Spectrophotometry, Infrared, pubmed-meshheading:20815000-Static Electricity
pubmed:year	2010
pubmed:articleTitle	Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics.
pubmed:affiliation	Department of Chemistry, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural