Nicholas Attila Kovacs

Nicholas is interested in the structural evolution of ribosomal proteins. Nicholas’ structure-based approaches have shown that segments of ribosomal proteins reveal the history of protein folding which stretches back since the origin of life. The data support a model in which (i) short, random coil polypeptides accreted onto the surface of the ribosome, and (ii) lengthened over time and coalesced into β-structures. (iii) These β-structures then collapsed, primarily into β-domains. (iv) Domains accumulated and gained complex super-secondary structures composed of both α-helix and β-strands. Life then diversified into its 3 domains and ribosomal proteins accrued elaborations on their structures. (v) In Archaea and Eukarya, insertions in ribosomal proteins gave rise to internal loop protrusions from their globular domains composed of unstructured segments as well as α-helices which buried into ribosomal RNA structure and made contacts with other ribosomal proteins. (vi) In Eukarya, α-helical extensions on the termini of ribosomal proteins gave rise to intricate ribosomal protein-ribosomal protein interactions on the surface of the ribosome.