1997年6月
Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study
LIFE SCIENCES
- ,
- ,
- ,
- 巻
- 61
- 号
- 4
- 開始ページ
- 411
- 終了ページ
- 418
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/S0024-3205(97)00398-6
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
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 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.
- リンク情報
- ID情報
-
- DOI : 10.1016/S0024-3205(97)00398-6
- ISSN : 0024-3205
- Web of Science ID : WOS:A1997XG97100008