| Autor: |
Debelle, Laurent, Alix, Alain J. P., Wei, Shao M., Jacob, Marie-Paule, Huvenne, Jean-Pierre, Berjot, Maurice, Legrand, Pierre |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; Dec98 Part 1, Vol. 258 Issue 2, p533-539, 7p, 4 Diagrams, 1 Chart, 1 Graph |
| Abstrakt: |
The presented work constitutes the first structural characterization of both insoluble human elastin and its solubilized form, κ-elastin. Structural data were reached following the use of Fourier transform infrared, near infrared Fourier transform Raman and circular dichroism optical spectroscopic methods and their quantitative analysis permitted us to estimate ≈10 % α-helices, ≈35 % β-strands and ≈55 % undefined conformations in the global secondary structure of insoluble human elastin in the solid state. Following the use of the LINK method, the probable local distribution of the secondary-structure elements along the sequence was determined and compared to that obtained for bovine elastin, the historical standard of elastin. This comparison led us to propose a globular architecture for the human elastomer and permitted us to delineate some elements of its structure-elasticity relationship. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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