| Autor: |
Hammond MS; Department of Chemistry, University of Waterloo, ON, Canada., Houliston RS, Meiering EM |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry and cell biology = Biochimie et biologie cellulaire [Biochem Cell Biol] 1998; Vol. 76 (2-3), pp. 294-301. |
| DOI: |
10.1139/bcb-76-2-3-294 |
| Abstrakt: |
We have used two-dimensional 1H-15N heteronuclear single quantum correlation spectroscopy to measure the pH dependence of backbone amide group chemical shifts in the actin binding protein hisactophilin over the pH range 5.7-11.1. Most of the resonances can be analyzed using a simple equation involving a single apparent ionization constant, pK(app). The majority of resonances in the protein titrate with pK(app) values of 5.6-7.4. The results can be rationalized in terms of titration of many histidine residues in hisactophilin. The titration data provide direct experimental support for the proposed models of the atomic basis of actin and membrane binding by hisactophilin. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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