What is it about?
We have analyzed the structural and physicochemical properties of protein-protein (PP), protein-RNA (PR) and RNA-RNA (RR) interfaces in small and large subunits of ribosomes, as well as in between the two subunits. Additionally, we have also developed Random Forest (RF) classifier to catalog the r-proteins.
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Why is it important?
Interactions between macromolecules play a crucial role in ribosome assembly that follows a highly coordinated process involving RNA folding and binding of ribosomal proteins (r-proteins). we have used Random Forest (RF) classifier to catalog the r-proteins in the ribosomal assemblies that support the hypothesis that large PR interfaces form first and promote the assembly to a higher order.
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This page is a summary of: Dissecting macromolecular recognition sites in ribosome: implication to its self-assembly, RNA Biology, June 2019, Taylor & Francis,
DOI: 10.1080/15476286.2019.1629767.
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