4425394

Source:http://linkedlifedata.com/resource/pubmed/id/4425394

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0028612, umls-concept:C0086486, umls-concept:C1280500, umls-concept:C1704241, umls-concept:C1705165, umls-concept:C2700061
pubmed:issue	8
pubmed:dateCreated	1975-1-16
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0372525
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/Nucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides
pubmed:status	MEDLINE
pubmed:issn	0006-3525
pubmed:author	pubmed-author:BrandBB, pubmed-author:ChangCC, pubmed-author:LiH JHJ, pubmed-author:RotterAA, pubmed-author:WeiskopfMM
pubmed:issnType	Print
pubmed:volume	13
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1681-97
pubmed:dateRevised	2008-11-21
pubmed:meshHeading	pubmed-meshheading:4425394-Animals, pubmed-meshheading:4425394-Binding Sites, pubmed-meshheading:4425394-Cattle, pubmed-meshheading:4425394-DNA, pubmed-meshheading:4425394-DNA, Bacterial, pubmed-meshheading:4425394-Hot Temperature, pubmed-meshheading:4425394-Hydrogen-Ion Concentration, pubmed-meshheading:4425394-Lysine, pubmed-meshheading:4425394-Methods, pubmed-meshheading:4425394-Molecular Conformation, pubmed-meshheading:4425394-Nucleoproteins, pubmed-meshheading:4425394-Peptides, pubmed-meshheading:4425394-Protein Binding, pubmed-meshheading:4425394-Protein Denaturation, pubmed-meshheading:4425394-Thymus Gland
pubmed:year	1974
pubmed:articleTitle	Helix-coil transition in nucleoprotein. Effect of ionic strength on thermal denaturation of polylysine-DNA complexes.
pubmed:publicationType	Journal Article