The relationship between protein domains and homopeptides in the Plasmodium falciparum proteome
The proteome of the malaria parasite Plasmodium falciparum is notable for the pervasive occurrence of homopeptides or low-complexity regions (i.e., regions that are made from a small subset of amino-acid residue types). The most prevalent of these are made from residues encoded by adenine/thymidine...
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Veröffentlicht in: | PeerJ (San Francisco, CA) CA), 2020-10, Vol.8, p.e9940-e9940, Article e9940 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The proteome of the malaria parasite
Plasmodium falciparum
is notable for the pervasive occurrence of homopeptides or low-complexity regions (i.e., regions that are made from a small subset of amino-acid residue types). The most prevalent of these are made from residues encoded by adenine/thymidine (AT)-rich codons, in particular asparagine. We examined homopeptide occurrences within protein domains in
P. falciparum
. Homopeptide enrichments occur for hydrophobic (e.g., valine), or small residues (alanine or glycine) in short spans ( |
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ISSN: | 2167-8359 2167-8359 |
DOI: | 10.7717/peerj.9940 |