Linked Life Data

14971914

Source:http://linkedlifedata.com/resource/pubmed/id/14971914

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2004-2-19
pubmed:abstractText
We used femtosecond infrared polarization spectroscopy and density functional theory in a study on the key signaling molecule nitric oxide (NO) bound to myoglobin. Our results show that after photolysis, a substantial fraction of NO recombines within the first few picoseconds. We discovered that the diatomic ligand is severely tilted in the protein and present evidence that the Fe-NO moiety can sample a wide range of off-axis tilting and bending conformations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1930-1
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
NO-bound myoglobin: structural diversity and dynamics of the NO ligand.
pubmed:affiliation
Department of Bioinformatics, University of Wuerzburg, Am Hubland, D-97074 Wuerzburg, Germany. zemojtel@biozentrum.uni-wuerzburg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't