Linked Life Data

19939563

Source:http://linkedlifedata.com/resource/pubmed/id/19939563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2010-2-1
pubmed:abstractText
The interaction between lysozyme and anthraquinone dyes such as Alizarin Red S, Acid blue 129 and Uniblue was studied using steady state, time resolved fluorescence measurements and docking studies. Addition of anthraquinone dyes effectively quenched the intrinsic fluorescence of lysozyme. Fluorescence quenching of lysozyme by dyes has revealed the formation of complex. The number of binding sites (n) and binding constant (K) for all the three dyes was calculated by relevant fluorescence quenching data. Based on Förster's non-radiative energy transfer theory, distance (r(0)) between the donor (lysozyme) and acceptor (dyes) as well as the critical energy transfer distance (R(0)) has also been calculated. The interaction between dyes and lysozyme occurs through static quenching mechanism as confirmed by time resolved spectroscopy. The conformational change of lysozyme has been analyzed using synchronous fluorescence measurement. Finally, docking studies revealed that specific interactions were observed with the residue of Trp 62.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1873-3336
pubmed:author
pubmed:copyrightInfo
(c) 2009 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
175
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
985-91
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Interaction of anthraquinone dyes with lysozyme: evidences from spectroscopic and docking studies.
pubmed:affiliation
School of Chemistry, Bharathidasan University, Tiruchirappalli 620024, Tamil Nadu, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't