Linked Life Data

16262335

Source:http://linkedlifedata.com/resource/pubmed/id/16262335

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2005-11-2
pubmed:abstractText
Immobilization and imaging of protein molecules and protein-DNA complexes on a Langmuir-Blodgett (LB) substrate have been explored here. We have prepared a nickel-arachidate (NiA) monolayer and characterized it through pressure-area isotherm on a LB trough. Recombinant RNA polymerase from Escherichia coli, where the largest subunit was replaced with the same gene having a series of histidine amino acids at the C-terminus end of the protein, was immobilized over the Ni-arachidate monolayer through a Ni(II)-histidine interaction. A single molecule of RNA polymerase could be seen through intermittent-contact atomic force microscopy (AFM). Under the condition of the formation of the LB monolayer, the enzyme molecules were arrayed and transcriptionally active. Interestingly, they could pick up sequence specific DNA molecules from the subphase in an oriented fashion. On the other hand, preformed RNA polymerase Ni(II)-arachidate monolayers bound DNA haphazardly when no surface pressure was employed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0743-7463
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10671-5
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Langmuir monolayer as a tool toward visualization of a specific DNA-protein complex.
pubmed:affiliation
Department of Physics and Molecular Biophysics Unit, Indian Institute of Science, Banglaore.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't