In contrast to the conventional paradigm that protein functions are determined by their structure encoded by the amino acid sequence, the IDRs confer protein functions without a stable three-dimensional structure through mechanisms that are harder to predict.
Comprising more than 30% of the human proteome, it is becoming increasingly important to determine the molecular mechanism of IDRs in essential cellular processes, including gene expression.
Recent advances have highlighted the role of the IDRs in cellular organisation by driving the formation of membraneless compartments, termed the biomolecular condensates. The IDRs contribute to forging large interaction networks among proteins and RNA molecules that undergo phase separation to form condensates.
We use a muti-pronged approach by combining spectroscopy, microscopy and atomistic simulations.