title: Structural protein reorganization and fold emergence investigated through amino acid sequence permutations.
abstract: Correlation between random amino acid sequences and protein folds suggests that proteins autonomously evolved the most stable folds, with stability and function evolving subsequently, suggesting the existence of common protein ancestors from which all modern proteins evolved. To test this hypothesis, we shuffled the sequences of 10 natural proteins and obtained 40 different and apparently unrelated folds. Our results suggest that shuffled sequences are sufficiently stable and may act as a basis to evolve functional proteins. The common secondary structure of modern proteins is well represented by a small set of permuted sequences, which also show the emergence of intrinsic disorder and aggregation-prone stretches of the polypeptide chain.
authors.affiliation: Department of Biomedical Sciences, University of Padova, Viale G. Colombo 3, 35131, Padua, Italy.
authors.forename: Giovanni
authors.initials: G
authors.lastname: Minervini
authors.forename: Alessandro
authors.initials: A
authors.lastname: Masiero
authors.forename: Emilio
authors.initials: E
authors.lastname: Potenza
authors.forename: Silvio C E
authors.initials: SC
authors.lastname: Tosatto
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins