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Intrinsically disordered proteins participate in many biological processes byfolding upon binding with other proteins. However, coupled folding and bindingprocesses are not well understood from an atomistic point of view. One of themain questions is whether folding occurs prior to or after binding. Here we usea novel unbiased high-throughput adaptive sampling approach to reconstruct thebinding and folding between the disordered transactivation domain of\mbox{c-Myb} and the KIX domain of the CREB-binding protein. The reconstructedlong-term dynamical process highlights the binding of a short stretch of aminoacids on \mbox{c-Myb} as a folded $\alpha$-helix. Leucine residues, speciallyLeu298 to Leu302, establish initial native contacts that prime the binding andfolding of the rest of the peptide, with a mixture of conformational selectionon the N-terminal region with an induced fit of the C-terminal.

Binding-and-folding recognition of an intrinsically disordered protein using online learning molecular dynamics