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| Content Provider | Springer Nature Link |
|---|---|
| Author | Fonin, A. V. Stepanenko, Olga V. Turoverov, K. K. Vorobyev, V. I. |
| Copyright Year | 2011 |
| Abstract | The fundamental possibility of interactions between non-histone chromatin protein HMGB1 and linker histone H1 in solutions with different ionic strengths was studied by intrinsic UV fluorescence, far and near UV CD, and spectrophotometry. The data we obtained allow us to assume that the increase in the histone H1 content in HMGB1 solutions with low ionic strengths is accompanied by the destruction of HMGB1 associates. The interactions between HMGB1 and H1 proteins increase the number of ordered regions in the protein molecules and causes slight changes in the tertiary structure of the protein. |
| Starting Page | 120 |
| Ending Page | 122 |
| Page Count | 3 |
| File Format | |
| ISSN | 1990519X |
| Journal | Cell and Tissue Biology |
| Volume Number | 5 |
| Issue Number | 2 |
| e-ISSN | 19905203 |
| Language | English |
| Publisher | SP MAIK Nauka/Interperiodica |
| Publisher Date | 2011-05-06 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | non-histone protein HMGB1 linker histone H1 chromatin protein folding intrinsically disordered protein Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology |
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