Linked Life Data

12928115

Source:http://linkedlifedata.com/resource/pubmed/id/12928115

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-8-20
pubmed:abstractText
Two physico-chemical perturbations were applied to ECFP, EGFP, EYFP and DsRed fluorescent proteins: high hydrostatic pressure and encapsulation in reversed micelles. The observed fluorescence changes were described by two-state model and quantified by thermodynamic formalism. ECFP, EYFP and DsRed exhibited similar reaction volumes under pressure. The changes of the chemical potentials of the chromophore in bis(2-ethylhexyl)sulfosuccinate (AOT) micelles caused apparent chromophore protonation changes resulting in a fluorescence decrease of ECFP and EYFP. In contrast to the remarkable stability of DsRed, the highest sensitivity of EYFP fluorescence under pressure and in micelles is attributed to its chromophore structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
1622
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Effect of high pressure and reversed micelles on the fluorescent proteins.
pubmed:affiliation
Department of Pharmacology, C236, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, CO 80262, USA. vlad.verkhusha@uchsc.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't