• Task 3.1 – IDR functional ontology: elucidating protein function described in the PED database which includes proteins with dynamically changing native conformations, also known as structural ensembles.
• Task 3.2 – NMR derived IDR analysis:NMR secondary chemical shifts represent an alternative source of information including statistical information about the dynamics of local structures. Task 3.2 will provide a detailed analysis and comparison with PED data to highlight differences and similarities.
• Task 3.3 – Linear motif covariation analysis: Covariation analysis is the amount of variation in multiple-sequence alignments which can be explained by constraints due to structural proximity. In the case of linear motifs (LMs) in IDPs, covariance will be measured between LMs and the interaction pockets of the protein domains it is bound to
• Task 3.4 – Analyze allostery-disorder transitions: an analysis of allosteric behavior.
• Task 3.5 – IDR domain covariation analysis: an analysis of covariation analysis For longer IDR regions known as “disordered domains”. Covariance will be measured and analysed for the region itself. and repetition.
• Task 3.6 – Describe fuzzy complexes: an analysis on protein complexes exploiting IDRs involved in “fuzzy” binding. The latter are not fully understood and overlap with IDRs driving phase-transitions. Starting from FuzzDB examples, the analysis will extend to cases identified in WP1 as well as from the relevant literature.

Deliverables