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- W3130414178 abstract "In the regime of domain classifications, the protein universe unveils a discrete set of folds connected by hierarchical relationships. Instead, at sub-domain-size resolution and because of physical constraints not necessarily requiring evolution to shape polypeptide chains, networks of protein motifs depict a continuous view that lies beyond the extent of hierarchical classification schemes. A number of studies, however, suggest that universal sub-sequences could be the descendants of peptides emerged in an ancient pre-biotic world. Should this be the case, evolutionary signals retained by structurally conserved motifs, along with hierarchical features of ancient domains, could sew relationships among folds that diverged beyond the point where homology is discernable. In view of the aforementioned, this paper provides a rationale where a network with hierarchical and continuous levels of the protein space, together with sequence profiles that probe the extent of sequence similarity and contacting residues that capture the transition from pre-biotic to domain world, has been used to explore relationships between ancient folds. Statistics of detected signals have been reported. As a result, an example of an emergent sub-network that makes sense from an evolutionary perspective, where conserved signals retrieved from the assessed protein space have been co-opted, has been discussed." @default.
- W3130414178 created "2021-03-01" @default.
- W3130414178 creator A5036757470 @default.
- W3130414178 date "2021-02-01" @default.
- W3130414178 modified "2023-10-17" @default.
- W3130414178 title "Fine tuned exploration of evolutionary relationships within the protein universe" @default.
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- W3130414178 doi "https://doi.org/10.1515/sagmb-2019-0039" @default.
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- W3130414178 hasPublicationYear "2021" @default.
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