Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-11-5
pubmed:abstractText
The interactions of recombinant juvenile hormone binding protein (His8-rJHBP) with juvenile hormones (JHs), methoprene and farnesol have been studied with electrochemical impedance spectroscopy (EIS). The protein was immobilized on the dodecanethiol (DDT) modified gold electrodes. Each step of electrode modification has been confirmed with cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). The conformation changes of His8-rJHBP upon JHs and methoprene binding have been presented. The EIS determined association constants in the JHs analogs-immobilized His8-rJHBP system indicate that lack of the epoxide moiety in methoprene molecule is not critical for observed high affinity of this compound to the binding region of the His8-rJHBP protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1093-4715
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2866-74
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Electrochemical impedance spectroscopy for the study of juvenile hormones-recombinant protein interactions.
pubmed:affiliation
Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Tuwima 10, 10-747 Olsztyn, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't