Matthew Merski, IEB
Conservation and Evolution of Protein Oligopeptide Repeats
Protein oligopeptide repeats are short (20-50 residue) sections of a protein that have a recognizable set of conserved sequence positions and have a common secondary structure pattern that occur as multiple copies within a single protein chain. Famous examples include TPR, WD40, and Ankyrin repeats. However, oligopeptide repeats often defy easy definition, with variations in their sequence length and/or composition making related repeats often appear unrelated. Oligopeptide repeats can confound sequence analyses because the repetitions in their short amino acid sequences lead to difficulties in identifying whether similar repeats are related (convergent evolution) or appear similar due to statistical chance (divergent evolution), even when comparing apparently orthologous proteins from related species. We have developed a fast and efficient method to analyze repeat proteins in an attempt to obviate these issues. Our results show that this kind of analysis can efficiently be applied to analyze repeat proteins on a large scale. I will present several examples highlighting our ability to detect and analyze these relationships in proteins that contain overlooked (cryptic) oligopeptide repeats despite both the sequence and structure of these proteins being known for 20 years.
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