Linked Life Data

21767504

Source:http://linkedlifedata.com/resource/pubmed/id/21767504

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-7-19
pubmed:abstractText
This work describes a detailed quantitative interaction study between the novel plastidial chaperone receptor OEP61 and isoforms of the chaperone types Hsp70 and Hsp90 using the optical method of total internal reflection ellipsometry (TIRE). The receptor OEP61 was electrostatically immobilized on a gold surface via an intermediate layer of polycations. The TIRE measurements allowed the evaluation of thickness changes in the adsorbed molecular layers as a result of chaperone binding to receptor proteins. Hsp70 chaperone isoforms but not Hsp90 were shown to be capable of binding OEP61. Dynamic TIRE measurements were carried out to evaluate the affinity constants of the above reactions and resulted in clear discrimination between specific and nonspecific binding of chaperones as well as differences in binding properties between the highly similar Hsp70 isoforms.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1542-0086
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
20
pubmed:volume
101
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
504-11
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry.
pubmed:affiliation
Biomedical Research Centre, Sheffield Hallam University, Sheffield, United Kingdom. v.kriechbaumer@shu.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't