Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study

P. Csermely, Yoshihiko Miyata, C. Söti, Ichiro Yahara

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The 90 kDa heat shock protein (hsp90) is a major cytoplasmic molecular chaperon 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 histone, the 'native molten globule', casein and calmodulin to hsp90 decrease in the order of K(d) = 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.

Original languageEnglish
Pages (from-to)411-418
Number of pages8
JournalLife Sciences
Volume61
Issue number4
DOIs
Publication statusPublished - Jun 20 1997

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Molecular Chaperones
Surface Plasmon Resonance
Surface plasmon resonance
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Carrier Proteins
HSP90 Heat-Shock Proteins
Steroid Receptors
Calmodulin
Heat-Shock Proteins
Caseins
Histones
Molten materials
Numerical analysis
Proteins

Keywords

  • Calmodulin
  • Casein
  • Histones
  • hsp90
  • Molecular chaperones
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Pharmacology

Cite this

Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study. / Csermely, P.; Miyata, Yoshihiko; Söti, C.; Yahara, Ichiro.

In: Life Sciences, Vol. 61, No. 4, 20.06.1997, p. 411-418.

Research output: Contribution to journalArticle

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