Linked Life Data

19666222

Source:http://linkedlifedata.com/resource/pubmed/id/19666222

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2009-8-26
pubmed:abstractText
To explore the impact of global incorporation of fluorinated aromatic amino acids on protein function, we investigated the effects of three monofluorinated phenylalanine analogs para-fluorophenylalanine (pFF), meta-fluorophenylalanine (mFF), and ortho-fluorophenylalanine (oFF) on the stability and enzymatic activity of the histone acetyltransferase (HAT), tGCN5. We selected this set of fluorinated amino acids because they bear the same size and overall polarity but alter in side chain shape and dipole direction. Our experiments showed that among three fluorinated amino acids, the global incorporation of pFF affords the smallest perturbation to the structure and function of tGCN5.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1464-3405
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5449-51
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Positional effects of monofluorinated phenylalanines on histone acetyltransferase stability and activity.
pubmed:affiliation
Department of Chemical and Biological Sciences, Polytechnic Institute of New York University, Brooklyn, NY 11201, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't