Dissection of human tropoelastin: exon-by-exon chemical synthesis and related conformational studies.

Antonio M Tamburro, Brigida Bochicchio, Antonietta Pepe

Journal: Biochemistry 2004;42(45):13347-62

PMID: 14609345

Full Text on American Chemical Society View on PubMed

Abstract

Polypeptide sequences encoding the single exons of human tropoelastin were synthesized and their conformations were studied in different solvents and at different temperatures by CD and (1)H NMR. The results demonstrated the presence of labile conformations such as poly-proline II helix (PPII) and beta-turns whose stability is strongly dependent on the microenvironment. Stable, periodic structures, such as alpha-helices, are only present in the poly-alanine cross-linking domains. These findings give a strong experimental basis to the understanding of the molecular mechanism of elasticity of elastin. In particular, they strongly support the description of the native relaxed state of the protein in terms of trans-conformational equilibria between extended and folded structures as previously proposed [Debelle, L., and Tamburro, A. M. (1999) Int. J. Biochem. Cell. Biol. 31, 261-272].

Address: Department of Chemistry, Università della Basilicata, Via N. Sauro 85, 85100 Potenza, Italy. [email protected]

DOI: 10.1021/bi034837t

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MeSH Terms: Amino Acid Sequence, Circular Dichroism, Elasticity, Exons, Glycine, Humans, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Lysine, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Proline, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Solutions, Structure-Activity Relationship, Tropoelastin, Water