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- Title
Protein secondary structure appears to be robust under in silico evolution while protein disorder appears not to be.
- Authors
Schaefer, Christian; Schlessinger, Avner; Rost, Burkhard
- Abstract
The mutation of amino acids often impacts protein function and structure. Mutations without negative effect sustain evolutionary pressure. We study a particular aspect of structural robustness with respect to mutations: regular protein secondary structure and natively unstructured (intrinsically disordered) regions. Is the formation of regular secondary structure an intrinsic feature of amino acid sequences, or is it a feature that is lost upon mutation and is maintained by evolution against the odds? Similarly, is disorder an intrinsic sequence feature or is it difficult to maintain? To tackle these questions, we in silico mutated native protein sequences into random sequence-like ensembles and monitored the change in predicted secondary structure and disorder.
- Publication
Bioinformatics (Oxford, England), 2010, Vol 26, Issue 5, p625
- ISSN
1367-4811
- Publication type
Journal Article
- DOI
10.1093/bioinformatics/btq012