ABSTRACT
Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to YPrA 266 Coupled Folding and Binding of Intrinsically Disordered Histone Chaperone Chz1 and Histone H2A.Z-H2B 269 Folding and Binding of Multiple Domains within a Multidomain Protein 272 Functional Landscape of ADK Modulated by Its Natural Substrates 274
Conclusions 277 Acknowledgments 278 References 278
Proteins realize their functions via interacting with other biomelecules. A classical example is the binding of a protein and its substrates during enzyme catalysis. To describe such a process, a lock and key notion was originally proposed by Emil Fischer more than a century ago (Fischer 1894). Subsequently, the lock and key mechanism was extended to explain the rigid biomolecular docking. However, the rigid body assumption was challenged by increasing evidence that biomolecular binding is often accompanied by local or global conformational adjustment of the proteins as well as their partners. is highlights the importance of conformational exibility in protein function and has led to a new relationship between function, structure, and dynamics. In particular, a class of proteins have been found to be able to carry out their functions without the need of well-dened structures under physiological conditions. ese proteins are known as intrinsically disordered proteins (IDPs). IDPs often change their conformations signicantly when binding to their partners, giving a hint that the exibility or dynamics should also determine the realization of function (Dunker et al. 2001; Dyson and Wright 2002, 2005; Papoian 2008; Wright and Dyson 1999).
