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Folding of polypeptide chains induced by the amino acid side-chains

par Ralston, Evelyn ;De Coen, Jean-Louis
Référence Journal of Molecular Biology, 83, 3, page (393-420)
Publication Publié, 1974-03

Article révisé par les pairs

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Résumé :

Conformational calculations with the use of semi-empirical potential functions have been applied to the analysis of the folding of peptide chains. In particular, the part played by the amino acid side-chains in the adoption of folded conformations has been investigated. The results show that the preferred conformations of short peptides are mostly extended ones. However, from a given peptide chain-length, the side-chain to backbone and side-chain to side-chain interactions become strong enough so that definite sequences of amino acids can induce a transition from extended to folded conformations. We propose to call these folded structures "conformational nuclei". The type of "nucleus" formed is dependent on both the amino acid composition and the sequence. Our results strongly support the hypothesis that folding of polypeptide chains can occur through a nucleation process that could be induced by the side-chains. © 1974.