Intrinsically disordered proteins lack stable tertiary and/or secondary 
structures under physiological conditions in vitro. Intrinsically disordered 
proteins undergo significant conformational transitions to well folded forms 
only on binding to partner. Molecular dynamics simulations are used to research 
the mechanism of folding for intrinsically disordered protein upon partner 
binding. Room-temperature MD simulations suggest that the intrinsically 
disordered proteins have nonspecific and specific interactions with the partner. 
Kinetic analysis of high-temperature MD simulations shows that bound and 
apo-states unfold via a two-state process, respectively. Φ-value analysis can 
identify the key residues of intrinsically disordered proteins. 
Kolmogorov-Smirnov (KS) P test analysis illustrates that the specific 
recognition between intrinsically disordered protein and partner might follow 
induced-fit mechanism. Furthermore, these methods can be widely used for the 
research of the binding induced folding for intrinsically disordered proteins.