| Autor: |
V N, Uverskiĭ, S E, Permiakov, I I, Senin, A M, Cherskaia, S V, Shul'ga-Morskoĭ, D V, Zinchenko, A M, Alekseev, A A, Zargarov, V M, Lipkin, P P, Filippov, E A, Permiakov |
| Rok vydání: |
2000 |
| Předmět: |
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| Zdroj: |
Bioorganicheskaia khimiia. 26(3) |
| ISSN: |
0132-3423 |
| Popis: |
The structural properties of myristoylated forms of recombinant recoverin of the wild type and of its mutants with damaged second and/or third Ca(2+)-binding sites were studied by fluorimetry and circular dichroism. The interaction of wild-type recoverin with calcium ions was shown to induce unusual structural rearrangements in its molecule. In particular, protein binding with Ca2+ ions results in an increase in the mobility of the environment of Trp residues, in higher hydrophobicity, and in elevated thermal stability (its thermal transition shifts by 15 degrees C to higher temperatures) but has almost no effect on its secondary structure. Similar structural changes induced by Ca2+ are also characteristic of the -EF2 mutant of recoverin whose second Ca(2+)-binding site is modified and cannot bind calcium ions. The structural properties of the -EF3 and -EF2,3 mutants (whose third or simultaneously second and third Ca(2+)-binding sites, respectively, are modified and damaged) are practically indifferent to calcium ions. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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