| Autor: |
J, Pagnier, M T, Bihoreau, V, Baudin, S J, Edelstein, C, Poyart |
| Jazyk: |
francouzština |
| Rok vydání: |
1993 |
| Předmět: |
|
| Zdroj: |
Comptes rendus de l'Academie des sciences. Serie III, Sciences de la vie. 316(4) |
| ISSN: |
0764-4469 |
| Popis: |
The Hb S (beta 6 Glu--Val) fiber is formed by the packing of double strands which constitute the basic unit of the deoxyHb S polymer. The specific interaction responsible for the stabilization of the double strand involves the mutated beta 6 Val side chain (lateral contact). Recombinant Hb beta 6 Glu--Ala and the double mutant beta 6 Glu--Ala, 23 Val--Ile exhibit a decreased solubility compared to Hb A. While the Hb beta 6 Ala does not polymerize, the association of the beta 23 Val--Ile mutation at the axial contact allows the double mutant to polymerize. These results show that: (1) the hydrophobic interactions between donor and acceptor sites depend on both the hydrophobicity and the stereospecificity of the amino acid side chain at the beta 6 position; (2) increasing the hydrophobic interactions at the axial contact (connecting molecules along the same strand) result in an increased stability of the lateral contact between filaments. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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