Aqueous solution (CD in water) and solid state (FT-IR on a ZnSe window) spectra of bovine tropoelastin (BTPE) have been recorded and analysed in order to get additional insights into the molecular structure of its elastic elastin polymer. Conformational analyses evidenced high levels of both ordered and unordered secondary structures in the solid and solution states. The structural contents of BTPE were estimated to : α-helices ∼ 10 %, β-sheets ∼ 30 %, β-turns ∼ 20 % and coil ∼ 40 % (Kabsch and Sander definition). Moreover, CD experiments showed the possibility for the molecule to be folded in an all-β configuration with short and / or distorted sheets. As this structural features were formerly predicted for BTPE, our experimental data allowed us to suggest a similar folding for monomeric elastin. Our all-β structural proposal for BTPE is discussed according to bovine elastin structure-elasticity relationship. © 1995, All rights reserved.
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