| Autor: |
Falconi, M., Gualtieri, M. T., La Teana, A., Losso, M. A., Pon, C. L. |
| Předmět: |
|
| Zdroj: |
Molecular Microbiology; May1988, Vol. 2 Issue 3, p323-329, 7p |
| Abstrakt: |
The primary sequence of H-NS (136 amino acid residues, Mr = 15402), an abundant Escherichia coli DNA-binding protein, has been elucidated and its quaternary structure has been investigated by protein-protein cross-linking reactions. It was found that H-NS exists predominantly as a dimer, even at very low concentrations, but may form tetramers at higher concentrations and that the protein-protein interaction responsible for the dimerization is chiefly hydrophobic. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text