Linked Life Data

15740117

Source:http://linkedlifedata.com/resource/pubmed/id/15740117

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2005-3-2
pubmed:abstractText
The photodynamics of wtGFP have been studied by ultrafast time-resolved infrared spectroscopy (TIR). In addition to the expected bleaching and transient infrared absorption of bands associated with the chromophore, we observe the dynamics of the proton relay reaction in the protein. Protonation of a protein carboxylate group occurs on the tens of picoseconds time scale following photoexcitation. Comparison with data for mutant GFPs, in which excited-state proton transfer has been disabled, supports the assignment of the carboxylate to the side chain of E222, a component of the hydrogen bonding network that links the two ends of the chromophore. The TIR data show that the rate-limiting step in the proton relay is deprotonation of the chromophore.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2864-5
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Observation of excited-state proton transfer in green fluorescent protein using ultrafast vibrational spectroscopy.
pubmed:affiliation
Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't