Linked Life Data

16913796

Source:http://linkedlifedata.com/resource/pubmed/id/16913796

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2006-8-17
pubmed:abstractText
Photoinduced fluorescence quenching electron transfer from N,N-dimethyl aniline to different 7-amino coumarin dyes has been investigated in sodium dodecyl sulfate (SDS) micelles and in bovine serum albumin (BSA)-SDS protein-surfactant complexes using steady state and picosecond time resolved fluorescence spectroscopy. The electron transfer rate has been found to be slower in BSA-SDS protein-surfactant complexes compared to that in SDS micelles. This observation has been explained with the help of the "necklace-and-bead" structure formed by the protein-surfactant complex due to coiling of protein molecules around the micelles. In the correlation of free energy change to the fluorescence quenching electron transfer rate, we have observed that coumarin 151 deviates from the normal Marcus region, showing retardation in the electron transfer rate at higher negative free energy region. We endeavored to establish that the retardation in the fluorescence quenching electron transfer rate for coumarin 151 at higher free energy region is a result of slower rotational relaxation and slower translational diffusion of coumarin 151 (C-151) compared to its analogues coumarin 152 and coumarin 481 in micelles and in protein-surfactant complexes. The slower rotational relaxation and translational diffusion of C-151 are supposed to be arising from the different location of coumarin 151 compared to coumarin 152 and coumarin 481.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16607-17
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Photoinduced electron transfer in a protein-surfactant complex: probing the interaction of SDS with BSA.
pubmed:affiliation
Department of Chemistry, Indian Institute of Technology, Kharagpur 721 302, WB, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't