| Autor: |
Esipova NG, Ragulina LE, Davydova LI, Lobachev VM, Makeev VIu, Bogush VG, Tumanian VG, Debabov VG |
| Jazyk: |
ruština |
| Zdroj: |
Biofizika [Biofizika] 2009 May-Jun; Vol. 54 (3), pp. 389-95. |
| Abstrakt: |
The distribution of secondary structures along the polypeptide chains of spider proteins spidroins 1 and 2 and their recombinant analogs has been studied by statistical methods. It was found that these proteins in the monomolecular form contain only trace amounts of beta-structures. At the same time, the regions of the sequence including Ala and Gly are predicted as helical-containing (with alpha-helices and left-helices of polyproline II type). An analysis of literature data and our data obtained in this study shows that the main conformation of the polypeptide chain solutions of spidroins 1 and 2 and their recombinant analogs in water solutions is the left-helix of polyproline II type with some contaminations of alpha-helices and a very small share of beta-structures. The transition to the state with extended conformations, which are peculiar to mature filaments of spider webs, requires the dehydration of the polypeptide chain backbone. Thus, the genesis of beta-structure in spider web proteins is determined by the conditions of conformation transitions between the main regular conformations of the polypeptide chain backbone. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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