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Thermodynamic modeling reveals widespread multivalent binding by RNA-binding proteins
Author(s) -
Salma Sohrabi-Jahromi,
Johannes Söding
Publication year - 2021
Publication title -
bioinformatics
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btab300
Subject(s) - rna , rna binding protein , computational biology , binding site , binding selectivity , plasma protein binding , riboswitch , biology , sequence motif , bipartite graph , genetics , microbiology and biotechnology , computer science , dna , non coding rna , biochemistry , theoretical computer science , gene , graph
Understanding how proteins recognize their RNA targets is essential to elucidate regulatory processes in the cell. Many RNA-binding proteins (RBPs) form complexes or have multiple domains that allow them to bind to RNA in a multivalent, cooperative manner. They can thereby achieve higher specificity and affinity than proteins with a single RNA-binding domain. However, current approaches to de novo discovery of RNA binding motifs do not take multivalent binding into account.

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