21860447

Source:http://linkedlifedata.com/resource/pubmed/id/21860447

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0015450, umls-concept:C0033727, umls-concept:C0242414
pubmed:issue	9
pubmed:dateCreated	2011-8-23
pubmed:abstractText	A joint X-ray/neutron diffraction study has enabled the direct observation of a hydronium ion coordinated by three amino-acid residues of an enzyme. This sighting will affect our views on how enzymes transport and use protons.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101499734
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Onium Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protons, http://linkedlifedata.com/resource/pubmed/chemical/hydronium ion
pubmed:status	MEDLINE
pubmed:month	Sep
pubmed:issn	1755-4349
pubmed:author	pubmed-author:DavidsonVictor LVL
pubmed:issnType	Electronic
pubmed:volume	3
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	662-3
pubmed:meshHeading	pubmed-meshheading:21860447-Models, Molecular, pubmed-meshheading:21860447-Neutron Diffraction, pubmed-meshheading:21860447-Onium Compounds, pubmed-meshheading:21860447-Protein Conformation, pubmed-meshheading:21860447-Proteins, pubmed-meshheading:21860447-Protons, pubmed-meshheading:21860447-X-Ray Diffraction
pubmed:year	2011
pubmed:articleTitle	Ion-protein coordination: the many faces of a proton.
pubmed:publicationType	News