Linked Life Data

9244367

Source:http://linkedlifedata.com/resource/pubmed/id/9244367

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-8-12
pubmed:abstractText
The 90 kDa heat shock protein (hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins including steroid receptors. Here we provide the first numerical analysis of hsp90-target associations using surface plasmon resonance. Binding affinities of histones, the "native molten globule", casein and calmodulin to hsp90 decrease in the order of Kd = 70 +/- 24, 220 +/- 70 and 1800 +/- 600 nM, respectively. Analysis of the structure of binding proteins revealed that their binding affinity depends on both hydrophobicity and positive charges making the discriminative features of hsp90 similar to those of other molecular chaperones.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0024-3205
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
411-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study.
pubmed:affiliation
Department of Medical Chemistry, Semmelweis University, School of Medicine, Budapest, Hungary. csermely@puskin.sote.hu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't